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Escherichia coli K-12 substr. MG1655 Polypeptide: RNA polymerase, sigma 32 (sigma H) factor



Gene: rpoH Accession Numbers: EG10897 (EcoCyc), b3461, ECK3445

Synonyms: fam, hin, htpR, sigma H factor, sigma H, sigma 32, sigma 32 factor, σ32

Regulation Summary Diagram: ?

Component of: RNA polymerase sigma 32

Summary:
rpoH encodes σ32, the primary sigma factor controlling the heat shock response during log-phase growth. It is subject to tight control via a multivalent regulatory system that reponds to temperature and the abundance of misfolded proteins within the cell.

σ32 levels rise, plateau and then drop following a heat shock, causing a similar induction in expression in heat shock genes [Zhao05, Zhou88, Straus, Tobe84, Grossman84, Yura84, Yamamori82]. At elevated temperatures formation of Eσ32 is favoured over that of Eσ70; σ32 has greater affinity for RNA polymerase, core enzyme than σ70 at high temperatures [Blaszczak95]. Large-scale identification of Eσ32 transcriptional targets has been carried out [Zhao05, Nonaka06]. The consensus promoter for Eσ32 initiation is TNtCNCcCTTGAA at -35 and CCCCATtTa at -10, where lowercase letters indicate a tendency toward, but not an absolute requirement for, a certain nucleotide at that location [Cowing85, Koo09]. Notably, recent work indicates that Eσ32 may only be involved in the heat shock response that occurs during log-phase, aerobic growth, with entirely different systems accounting for heat shock responses during stationary phase and anaerobic growth [DiazAcosta06].

σ32 is also responsible for genetic responses to other environmental insults. Ethanol, alkaline pH changes and hyperosmotic shock all induce the σ32-dependent heat shock response [VanBogelen87, Taglicht87, Bianchi99]. In addition, σ32 is induced by carbon starvation [Jenkins91a].

σ32 regulation is a multivalent process consisting of transcriptional, translational and postranslational controls.

rpoH is transcribed from two constitutive σ70-driven promoters, as well as at least one heat-shock responsive promoter and one σ24-driven promoter [Erickson87, Fujita87a, Wang89a, Erickson89a]. Three of the rpoH promoters are suppressed by DnaA binding [Wang89]. rpoH transcription does not depend on σ32 [Tilly86].

σ32 abundance is regulated at the translational level via mRNA secondary structure. Two sequences in the rpoH mRNA, one near the translation start site and one internal, form a secondary structure element that is disrupted by higher temperatures, allowing translation [KamathLoeb91, Nagai91b, Yuzawa93, Morita99, Morita99a].

σ32 is regulated post-translationally via degradation and by direct inhibition of its activity [Grossman87]. Importantly, σ32 must be associated with the inner membrane to be properly regulated. Membrane localization of σ32 is facilitated by the signal recognition particle (SRP) translocation system although σ32 does not appear to contain a signal sequence nor any transmembrane regions. Fractionation experiments suggest that approximately 50% of σ32 is membrane associated [Lim13].

σ32 is a very unstable protein which is transiently stabilised upon heat shock [Grossman87, Straus, Tilly89, Morita00]. σ32 is stabilized in the absence of the chaperone protein GroES and by the presence of abnormal proteins [Kanemori94, Kanemori94a]. Degradation of σ32 depends on the ATP dependent protease FtsH and HslVU protease [Herman95, Kanemori97, Tatsuta98].

σ32 activity is directly controlled by the DnaK-DnaJ-GrpE chaperone system. When this chaperone system is occupied by substrates such as misfolded proteins, it is not available to bind σ32 and limit its activity [Gamer96, Tomoyasu98, Tatsuta98, Gamer92]. In this way, σ32 activity is tied directly to the level of misfolded proteins in the cell. CbpA and the GroEL-GroES chaperonin complex can also both limit σ32 activity in the same manner [Tatsuta98, Guisbert04]. σ32 binds DnaK in vitro [Liberek92]; σ32 contains multiple DnaK binding sites [Noguchi14]. DnaK, σ32 and DnaJ form a stable complex in vitro; efficient formation of the complex depends on the presence of ATP. DnaK and DnaJ compete with RNA polymerase core for stable binding to σ32[Liberek93]. The chaperones DnaK, DnaJ and GrpE interact with σ32 in vivo [Gamer92]. FtsH degrades σ32 present in a DnaK-σ32-DnaJ complex in vitro but is unable to degrade σ32 present in the Eσ32 complex [Blaszczak99].

A σ32 I54N mutant is defective for chaperone (DnaK/J, GroEL/S) mediated inactivation in vivo but shows no altered interaction with chaperones or RNA polymerase in vitro [Yura07]. A σ32 I54N mutant is defective in membrane association; artificially tethering this mutant to the membrane restores homeostatic control mediated by chaperones and FtsH [Lim13]

σ32 activity can also be attenuated via phosphorylation [Klein03].

Conserved region 2 of σ32 is heavily involved in its activity and regulation. Region 2.2 is involved in interaction with the RNA polymerase, core enzyme, along with other portions of the protein [Joo97, Joo98]. Region 2 is important for FtsH-mediated degradation [Bertani01]. σ32 becomes more flexible as temperature rises, and in particular region 2 appears to undergo a reversible unfolding [Rist03]. Region 2.1 is involved in σ32 stability and its transcriptional efficacy [Horikoshi04, Obrist05]. Region C (from L118 to R140) has been implicated in binding of DnaK [McCarty96], in high affinity binding to core RNA polymerase [Arsene99] and in FtsH mediated proteolysis [Obrist09].

rpoH mutants suffer a number of ills in addition to failure of the heat shock response. They are deficient in cell division at higher temperatures and sensitive to oxidative stress at any temperature [Tsuchido86, Kogoma92]. Both F and mini-F plasmid replication depend on σ32 and fail in its absence [Wada86a, Wada87a]. In rpoH mutants, newly synthesized protein aggregates readily even under normal growth conditions [Gragerov91].

σ32 has been evaluated via linker insertion mutational analysis [Narberhaus03].

Whereas Eσ70-directed transcription is rifampicin sensitive, Eσ32-directed transcription is partially rifampicin resistant [Wegrzyn98].

A σ-competition model based on comparative kinetic and thermodynamic properties was developed [Ganguly12].

Review: [Arsene00]
Comments: [Robinson13a, Busby09]

Citations: [Neidhardt83, Straus89, Suzuki12, Urech00, Meyer11]

Gene Citations: [Pallen99, Narberhaus96]

Locations: inner membrane, cytosol

Map Position: [3,597,952 <- 3,598,806] (77.55 centisomes)
Length: 855 bp / 284 aa

Molecular Weight of Polypeptide: 32.469 kD (from nucleotide sequence), 36 kD (experimental) [Tobe84 ]

Unification Links: ASAP:ABE-0011303 , CGSC:618 , DIP:DIP-46203N , EchoBASE:EB0890 , EcoGene:EG10897 , EcoliWiki:b3461 , ModBase:P0AGB3 , OU-Microarray:b3461 , PortEco:rpoH , PR:PRO_000023849 , Pride:P0AGB3 , Protein Model Portal:P0AGB3 , RefSeq:NP_417918 , RegulonDB:EG10897 , SMR:P0AGB3 , String:511145.b3461 , UniProt:P0AGB3

Relationship Links: InterPro:IN-FAMILY:IPR000943 , InterPro:IN-FAMILY:IPR007627 , InterPro:IN-FAMILY:IPR007630 , InterPro:IN-FAMILY:IPR011991 , InterPro:IN-FAMILY:IPR012759 , InterPro:IN-FAMILY:IPR013324 , InterPro:IN-FAMILY:IPR013325 , InterPro:IN-FAMILY:IPR014284 , Pfam:IN-FAMILY:PF04542 , Pfam:IN-FAMILY:PF04545 , Prints:IN-FAMILY:PR00046 , Prosite:IN-FAMILY:PS00715 , Prosite:IN-FAMILY:PS00716

In Paralogous Gene Group: 363 (4 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0001121 - transcription from bacterial-type RNA polymerase promoter Inferred by computational analysis Inferred from experiment [Liberek92, Cowing85, Grossman84]
GO:0006355 - regulation of transcription, DNA-templated Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01, Zhao05]
GO:0009408 - response to heat Inferred by computational analysis Inferred from experiment [Straus, Yamamori82, Yura84, Grossman84, GOA01]
GO:0010468 - regulation of gene expression Inferred by computational analysis Inferred from experiment [Yamamori82, GOA06]
GO:0001123 - transcription initiation from bacterial-type RNA polymerase promoter Inferred by computational analysis [GOA06]
GO:0006351 - transcription, DNA-templated Inferred by computational analysis [UniProtGOA11a]
GO:0006352 - DNA-templated transcription, initiation Inferred by computational analysis [GOA01]
GO:0006950 - response to stress Inferred by computational analysis [UniProtGOA11a, GOA06]
Molecular Function: GO:0000990 - core RNA polymerase binding transcription factor activity Inferred from experiment [Grossman84]
GO:0003677 - DNA binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01, Zhao05]
GO:0005515 - protein binding Inferred from experiment [Liberek92]
GO:0016987 - sigma factor activity Inferred by computational analysis Inferred from experiment [Grossman84, UniProtGOA11a, GOA06, GOA01]
GO:0003700 - sequence-specific DNA binding transcription factor activity Inferred by computational analysis [GOA01]
GO:0008270 - zinc ion binding Inferred by computational analysis [GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Lim13]
GO:0005886 - plasma membrane Inferred from experiment [Lim13]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06]

MultiFun Terms: cell processes adaptations temperature extremes
information transfer RNA related Transcription related
regulation genetic unit regulated stimulon
regulation type of regulation transcriptional level sigma factors, anti-sigmafactors

Essentiality data for rpoH knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Credits:
Curated 11-Aug-2006 by Shearer A , SRI International
Last-Curated ? 03-Sep-2014 by Mackie A , Macquarie University


Subunit of: RNA polymerase sigma 32

Synonyms: RNA polymerase sigma 32 holoenzyme, RNA polymerase sigma H

Subunit composition of RNA polymerase sigma 32 = [(RpoA)2(RpoC)(RpoB)][RpoH]
         RNA polymerase, core enzyme = (RpoA)2(RpoC)(RpoB) (extended summary available)
                 RNA polymerase, α subunit = RpoA (extended summary available)
                 RNA polymerase, β' subunit = RpoC (extended summary available)
                 RNA polymerase, β subunit = RpoB (summary available)
         RNA polymerase, sigma 32 (sigma H) factor = RpoH (extended summary available)

Controlled Transcription Units (97 total): ?

Notes:


Sequence Features

Feature Class Location Common Name Citations Comment State
Protein-Segment 53 -> 122  
[UniProt13]
UniProt: Sigma-70 factor domain-2; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.
 
Mutagenesis-Variant 54  
[Lim13]
Alternate sequence I → N; defective in membrane association
 
Conserved-Region 58 -> 90 Region 2
[Helmann88]
Conserved region 2; may be associated with recognition of core RNA polymerase
 
Protein-Segment 77 -> 80  
[UniProt13]
UniProt: Interaction with polymerase core subunit RpoC; Sequence Annotation Type: short sequence motif.
 
Mutagenesis-Variant 80  
[Joo97, UniProt13]
Alternate sequence: Q → R; UniProt: Decrease in activity. Exhibits reduced affinity for core RNAP.
Alternate sequence: Q → N; UniProt: Decrease in activity. Exhibits reduced affinity for core RNAP.
 
Protein-Binding-Region 118 -> 125  
DnaK binds to Sigma32 at this sequence [McCarty96].
 
Protein-Binding-Region 133 -> 140 RpoH box
[Tsujimura75]
DnaK binds to Sigma32 at this sequence [McCarty96];
 
Conserved-Region 149 -> 195 Region 3
[Helmann88]
conserved region 3; implicated in promoter recognition
 
Sequence-Conflict 185  
[Yura84, UniProt10]
Alternate sequence: S → A; UniProt: (in Ref. 3; AAA23991);
 
Sequence-Conflict 193 -> 194  
[Yura84, UniProt10]
Alternate sequence: QP → HA; UniProt: (in Ref. 3; AAA23991);
 
Protein-Segment 228 -> 280  
[UniProt13]
UniProt: Sigma-70 factor domain-4; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.
 
Conserved-Region 232 -> 284 Region 4
[Helmann88]
Coserved region 4; implicated in promoter recogntion
 
DNA-Binding-Region 253 -> 272  
[UniProt10a]
UniProt: H-T-H motif; Non-Experimental Qualifier: by similarity;
 
Phosphorylation-Modification 260  
Phosphorylation at this residue attenutes the transcriptional initiator activity of Sigma32 [Klein03].
Unmodified


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b3461 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10897; confirmed by SwissProt match.


References

Arsene00: Arsene F, Tomoyasu T, Bukau B (2000). "The heat shock response of Escherichia coli." Int J Food Microbiol 55(1-3);3-9. PMID: 10791710

Arsene99: Arsene F, Tomoyasu T, Mogk A, Schirra C, Schulze-Specking A, Bukau B (1999). "Role of region C in regulation of the heat shock gene-specific sigma factor of Escherichia coli, sigma32." J Bacteriol 181(11);3552-61. PMID: 10348869

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bertani01: Bertani D, Oppenheim AB, Narberhaus F (2001). "An internal region of the RpoH heat shock transcription factor is critical for rapid degradation by the FtsH protease." FEBS Lett 493(1);17-20. PMID: 11277997

Bianchi99: Bianchi AA, Baneyx F (1999). "Hyperosmotic shock induces the sigma32 and sigmaE stress regulons of Escherichia coli." Mol Microbiol 34(5);1029-38. PMID: 10594827

Blaszczak95: Blaszczak A, Zylicz M, Georgopoulos C, Liberek K (1995). "Both ambient temperature and the DnaK chaperone machine modulate the heat shock response in Escherichia coli by regulating the switch between sigma 70 and sigma 32 factors assembled with RNA polymerase." EMBO J 14(20);5085-93. PMID: 7588636

Blaszczak99: Blaszczak A, Georgopoulos C, Liberek K (1999). "On the mechanism of FtsH-dependent degradation of the sigma 32 transcriptional regulator of Escherichia coli and the role of the Dnak chaperone machine." Mol Microbiol 31(1);157-66. PMID: 9987118

Busby09: Busby SJ (2009). "More pieces in the promoter jigsaw: recognition of -10 regions by alternative sigma factors." Mol Microbiol 72(4);809-11. PMID: 19400800

Cowing85: Cowing DW, Bardwell JC, Craig EA, Woolford C, Hendrix RW, Gross CA (1985). "Consensus sequence for Escherichia coli heat shock gene promoters." Proc Natl Acad Sci U S A 82(9);2679-83. PMID: 3887408

DiazAcosta06: Diaz-Acosta A, Sandoval ML, Delgado-Olivares L, Membrillo-Hernandez J (2006). "Effect of anaerobic and stationary phase growth conditions on the heat shock and oxidative stress responses in Escherichia coli K-12." Arch Microbiol 185(6);429-38. PMID: 16775749

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Erickson87: Erickson JW, Vaughn V, Walter WA, Neidhardt FC, Gross CA (1987). "Regulation of the promoters and transcripts of rpoH, the Escherichia coli heat shock regulatory gene." Genes Dev 1(5);419-32. PMID: 3315851

Erickson89a: Erickson JW, Gross CA (1989). "Identification of the sigma E subunit of Escherichia coli RNA polymerase: a second alternate sigma factor involved in high-temperature gene expression." Genes Dev 3(9);1462-71. PMID: 2691330

Fujita87a: Fujita N, Ishihama A (1987). "Heat-shock induction of RNA polymerase sigma-32 synthesis in Escherichia coli: transcriptional control and a multiple promoter system." Mol Gen Genet 210(1);10-5. PMID: 3323832

Gamer92: Gamer J, Bujard H, Bukau B (1992). "Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor sigma 32." Cell 69(5);833-42. PMID: 1534276

Gamer96: Gamer J, Multhaup G, Tomoyasu T, McCarty JS, Rudiger S, Schonfeld HJ, Schirra C, Bujard H, Bukau B (1996). "A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32." EMBO J 15(3);607-17. PMID: 8599944

Ganguly12: Ganguly A, Chatterji D (2012). "A comparative kinetic and thermodynamic perspective of the σ-competition model in Escherichia coli." Biophys J 103(6);1325-33. PMID: 22995505

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Gragerov91: Gragerov AI, Martin ES, Krupenko MA, Kashlev MV, Nikiforov VG (1991). "Protein aggregation and inclusion body formation in Escherichia coli rpoH mutant defective in heat shock protein induction." FEBS Lett 291(2);222-4. PMID: 1936268

Grossman84: Grossman AD, Erickson JW, Gross CA (1984). "The htpR gene product of E. coli is a sigma factor for heat-shock promoters." Cell 38(2);383-90. PMID: 6380765

Grossman87: Grossman AD, Straus DB, Walter WA, Gross CA (1987). "Sigma 32 synthesis can regulate the synthesis of heat shock proteins in Escherichia coli." Genes Dev 1(2);179-84. PMID: 3315848

Guisbert04: Guisbert E, Herman C, Lu CZ, Gross CA (2004). "A chaperone network controls the heat shock response in E. coli." Genes Dev 18(22);2812-21. PMID: 15545634

Helmann88: Helmann JD, Chamberlin MJ (1988). "Structure and function of bacterial sigma factors." Annu Rev Biochem 57;839-72. PMID: 3052291

Herman95: Herman C, Thevenet D, D'Ari R, Bouloc P (1995). "Degradation of sigma 32, the heat shock regulator in Escherichia coli, is governed by HflB." Proc Natl Acad Sci U S A 1995;92(8);3516-20. PMID: 7724592

Horikoshi04: Horikoshi M, Yura T, Tsuchimoto S, Fukumori Y, Kanemori M (2004). "Conserved region 2.1 of Escherichia coli heat shock transcription factor sigma32 is required for modulating both metabolic stability and transcriptional activity." J Bacteriol 186(22);7474-80. PMID: 15516558

Jenkins91a: Jenkins DE, Auger EA, Matin A (1991). "Role of RpoH, a heat shock regulator protein, in Escherichia coli carbon starvation protein synthesis and survival." J Bacteriol 173(6);1992-6. PMID: 2002001

Joo97: Joo DM, Ng N, Calendar R (1997). "A sigma32 mutant with a single amino acid change in the highly conserved region 2.2 exhibits reduced core RNA polymerase affinity." Proc Natl Acad Sci U S A 94(10);4907-12. PMID: 9144163

Joo98: Joo DM, Nolte A, Calendar R, Zhou YN, Jin DJ (1998). "Multiple regions on the Escherichia coli heat shock transcription factor sigma32 determine core RNA polymerase binding specificity." J Bacteriol 180(5);1095-102. PMID: 9495746

KamathLoeb91: Kamath-Loeb AS, Gross CA (1991). "Translational regulation of sigma 32 synthesis: requirement for an internal control element." J Bacteriol 173(12);3904-6. PMID: 2050641

Kanemori94: Kanemori M, Mori H, Yura T (1994). "Effects of reduced levels of GroE chaperones on protein metabolism: enhanced synthesis of heat shock proteins during steady-state growth of Escherichia coli." J Bacteriol 176(14);4235-42. PMID: 7912695

Kanemori94a: Kanemori M, Mori H, Yura T (1994). "Induction of heat shock proteins by abnormal proteins results from stabilization and not increased synthesis of sigma 32 in Escherichia coli." J Bacteriol 176(18);5648-53. PMID: 7916010

Kanemori97: Kanemori M, Nishihara K, Yanagi H, Yura T (1997). "Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli." J Bacteriol 179(23);7219-25. PMID: 9393683

Klein03: Klein G, Dartigalongue C, Raina S (2003). "Phosphorylation-mediated regulation of heat shock response in Escherichia coli." Mol Microbiol 48(1);269-85. PMID: 12657060

Kogoma92: Kogoma T, Yura T (1992). "Sensitization of Escherichia coli cells to oxidative stress by deletion of the rpoH gene, which encodes the heat shock sigma factor." J Bacteriol 174(2);630-2. PMID: 1729253

Koo09: Koo BM, Rhodius VA, Campbell EA, Gross CA (2009). "Dissection of recognition determinants of Escherichia coli sigma32 suggests a composite -10 region with an 'extended -10' motif and a core -10 element." Mol Microbiol 72(4);815-29. PMID: 19400791

Liberek92: Liberek K, Galitski TP, Zylicz M, Georgopoulos C (1992). "The DnaK chaperone modulates the heat shock response of Escherichia coli by binding to the sigma 32 transcription factor." Proc Natl Acad Sci U S A 89(8);3516-20. PMID: 1565647

Liberek93: Liberek K, Georgopoulos C (1993). "Autoregulation of the Escherichia coli heat shock response by the DnaK and DnaJ heat shock proteins." Proc Natl Acad Sci U S A 90(23);11019-23. PMID: 8248205

Lim13: Lim B, Miyazaki R, Neher S, Siegele DA, Ito K, Walter P, Akiyama Y, Yura T, Gross CA (2013). "Heat Shock Transcription Factor σ(32) Co-opts the Signal Recognition Particle to Regulate Protein Homeostasis in E. coli." PLoS Biol 11(12);e1001735. PMID: 24358019

McCarty96: McCarty JS, Rudiger S, Schonfeld HJ, Schneider-Mergener J, Nakahigashi K, Yura T, Bukau B (1996). "Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria." J Mol Biol 256(5);829-37. PMID: 8601834

Meyer11: Meyer AS, Baker TA (2011). "Proteolysis in the Escherichia coli heat shock response: a player at many levels." Curr Opin Microbiol 14(2);194-9. PMID: 21353626

Morita00: Morita MT, Kanemori M, Yanagi H, Yura T (2000). "Dynamic interplay between antagonistic pathways controlling the sigma 32 level in Escherichia coli." Proc Natl Acad Sci U S A 97(11);5860-5. PMID: 10801971

Morita99: Morita M, Kanemori M, Yanagi H, Yura T (1999). "Heat-induced synthesis of sigma32 in Escherichia coli: structural and functional dissection of rpoH mRNA secondary structure." J Bacteriol 181(2);401-10. PMID: 9882652

Morita99a: Morita MT, Tanaka Y, Kodama TS, Kyogoku Y, Yanagi H, Yura T (1999). "Translational induction of heat shock transcription factor sigma32: evidence for a built-in RNA thermosensor." Genes Dev 13(6);655-65. PMID: 10090722

Nagai91b: Nagai H, Yuzawa H, Yura T (1991). "Interplay of two cis-acting mRNA regions in translational control of sigma 32 synthesis during the heat shock response of Escherichia coli." Proc Natl Acad Sci U S A 88(23);10515-9. PMID: 1961716

Narberhaus03: Narberhaus F, Balsiger S (2003). "Structure-function studies of Escherichia coli RpoH (sigma32) by in vitro linker insertion mutagenesis." J Bacteriol 185(9);2731-8. PMID: 12700252

Narberhaus96: Narberhaus F, Weiglhofer W, Fischer HM, Hennecke H (1996). "The Bradyrhizobium japonicum rpoH1 gene encoding a sigma 32-like protein is part of a unique heat shock gene cluster together with groESL1 and three small heat shock genes." J Bacteriol 1996;178(18);5337-46. PMID: 8808920

Neidhardt83: Neidhardt FC, VanBogelen RA, Lau ET (1983). "Molecular cloning and expression of a gene that controls the high-temperature regulon of Escherichia coli." J Bacteriol 153(2);597-603. PMID: 6337122

Noguchi14: Noguchi A, Ikeda A, Mezaki M, Fukumori Y, Kanemori M (2014). "DnaJ-promoted binding of DnaK to multiple sites on σ32 in the presence of ATP." J Bacteriol 196(9);1694-703. PMID: 24532774

Nonaka06: Nonaka G, Blankschien M, Herman C, Gross CA, Rhodius VA (2006). "Regulon and promoter analysis of the E. coli heat-shock factor, sigma32, reveals a multifaceted cellular response to heat stress." Genes Dev 20(13);1776-89. PMID: 16818608

Obrist05: Obrist M, Narberhaus F (2005). "Identification of a turnover element in region 2.1 of Escherichia coli sigma32 by a bacterial one-hybrid approach." J Bacteriol 187(11);3807-13. PMID: 15901705

Obrist09: Obrist M, Langklotz S, Milek S, Fuhrer F, Narberhaus F (2009). "Region C of the Escherichia coli heat shock sigma factor RpoH (sigma 32) contains a turnover element for proteolysis by the FtsH protease." FEMS Microbiol Lett 290(2);199-208. PMID: 19025566

Pallen99: Pallen M (1999). "RpoN-dependent transcription of rpoH?." Mol Microbiol 1999;31(1);393. PMID: 9987139

Rist03: Rist W, Jorgensen TJ, Roepstorff P, Bukau B, Mayer MP (2003). "Mapping temperature-induced conformational changes in the Escherichia coli heat shock transcription factor sigma 32 by amide hydrogen exchange." J Biol Chem 278(51);51415-21. PMID: 14504287

Robinson13a: Robinson R (2013). "Heat shock response regulator is pinned to the membrane." PLoS Biol 11(12);e1001736. PMID: 24358020

Straus: Straus DB, Walter WA, Gross CA "The heat shock response of E. coli is regulated by changes in the concentration of sigma 32." Nature 329(6137);348-51. PMID: 3306410

Straus89: Straus DB, Walter WA, Gross CA (1989). "The activity of sigma 32 is reduced under conditions of excess heat shock protein production in Escherichia coli." Genes Dev 3(12A);2003-10. PMID: 2695391

Suzuki12: Suzuki H, Ikeda A, Tsuchimoto S, Adachi K, Noguchi A, Fukumori Y, Kanemori M (2012). "Synergistic binding of DnaJ and DnaK chaperones to heat shock transcription factor σ32 ensures its characteristic high metabolic instability: implications for heat shock protein 70 (Hsp70)-Hsp40 mode of function." J Biol Chem 287(23);19275-83. PMID: 22496372

Taglicht87: Taglicht D, Padan E, Oppenheim AB, Schuldiner S (1987). "An alkaline shift induces the heat shock response in Escherichia coli." J Bacteriol 169(2);885-7. PMID: 3542975

Tatsuta98: Tatsuta T, Tomoyasu T, Bukau B, Kitagawa M, Mori H, Karata K, Ogura T (1998). "Heat shock regulation in the ftsH null mutant of Escherichia coli: dissection of stability and activity control mechanisms of sigma32 in vivo." Mol Microbiol 30(3);583-93. PMID: 9822823

Tilly86: Tilly K, Erickson J, Sharma S, Georgopoulos C (1986). "Heat shock regulatory gene rpoH mRNA level increases after heat shock in Escherichia coli." J Bacteriol 168(3);1155-8. PMID: 2430947

Tilly89: Tilly K, Spence J, Georgopoulos C (1989). "Modulation of stability of the Escherichia coli heat shock regulatory factor sigma." J Bacteriol 171(3);1585-9. PMID: 2646289

Tobe84: Tobe T, Ito K, Yura T (1984). "Isolation and physical mapping of temperature-sensitive mutants defective in heat-shock induction of proteins in Escherichia coli." Mol Gen Genet 195(1-2);10-6. PMID: 6092838

Tomoyasu98: Tomoyasu T, Ogura T, Tatsuta T, Bukau B (1998). "Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli." Mol Microbiol 30(3);567-81. PMID: 9822822

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Other References Related to Gene Regulation

Gavigan99: Gavigan SA, Nguyen T, Nguyen N, Senear DF (1999). "Role of multiple CytR binding sites on cooperativity, competition, and induction at the Escherichia coli udp promoter." J Biol Chem 1999;274(23);16010-9. PMID: 10347150

Holst92: Holst B, Sogaard-Andersen L, Pedersen H, Valentin-Hansen P (1992). "The cAMP-CRP/CytR nucleoprotein complex in Escherichia coli: two pairs of closely linked binding sites for the cAMP-CRP activator complex are involved in combinatorial regulation of the cdd promoter." EMBO J 11(10);3635-43. PMID: 1327747

Holt10: Holt AK, Senear DF (2010). "An unusual pattern of CytR and CRP binding energetics at Escherichia coli cddP suggests a unique blend of class I and class II mediated activation." Biochemistry 49(3);432-42. PMID: 20000490

Janaszak07: Janaszak A, Majczak W, Nadratowska B, Szalewska-Palasz A, Konopa G, Taylor A (2007). "A {sigma}54-dependent promoter in the regulatory region of the Escherichia coli rpoH gene." Microbiology 153(Pt 1);111-23. PMID: 17185540

Janaszak09: Janaszak A, Nadratowska-Wesolowska B, Konopa G, Taylor A (2009). "The P1 promoter of the Escherichia coli rpoH gene is utilized by sigma 70 -RNAP or sigma s -RNAP depending on growth phase." FEMS Microbiol Lett 291(1);65-72. PMID: 19076234

Jorgensen98: Jorgensen CI, Kallipolitis BH, Valentin-Hansen P (1998). "DNA-binding characteristics of the Escherichia coli CytR regulator: a relaxed spacing requirement between operator half-sites is provided by a flexible, unstructured interdomain linker." Mol Microbiol 27(1);41-50. PMID: 9466254

Kallipolitis98: Kallipolitis BH, Valentin-Hansen P (1998). "Transcription of rpoH, encoding the Escherichia coli heat-shock regulator sigma32, is negatively controlled by the cAMP-CRP/CytR nucleoprotein complex." Mol Microbiol 1998;29(4);1091-9. PMID: 9767576

Meibom00: Meibom KL, Kallipolitis BH, Ebright RH, Valentin-Hansen P (2000). "Identification of the subunit of cAMP receptor protein (CRP) that functionally interacts with CytR in CRP-CytR-mediated transcriptional repression." J Biol Chem 275(16);11951-6. PMID: 10766824

Nagai90: Nagai H, Yano R, Erickson JW, Yura T (1990). "Transcriptional regulation of the heat shock regulatory gene rpoH in Escherichia coli: involvement of a novel catabolite-sensitive promoter." J Bacteriol 1990;172(5);2710-5. PMID: 2139650

Pedersen97: Pedersen H, Valentin-Hansen P (1997). "Protein-induced fit: the CRP activator protein changes sequence-specific DNA recognition by the CytR repressor, a highly flexible LacI member." EMBO J 16(8);2108-18. PMID: 9155036

Perini96: Perini LT, Doherty EA, Werner E, Senear DF (1996). "Multiple specific CytR binding sites at the Escherichia coli deoP2 promoter mediate both cooperative and competitive interactions between CytR and cAMP receptor protein." J Biol Chem 271(52);33242-55. PMID: 8969182

Rhodius05: Rhodius VA, Suh WC, Nonaka G, West J, Gross CA (2005). "Conserved and variable functions of the sigmaE stress response in related genomes." PLoS Biol 4(1);e2. PMID: 16336047

SogaardAndersen90: Sogaard-Andersen L, Martinussen J, Mollegaard NE, Douthwaite SR, Valentin-Hansen P (1990). "The CytR repressor antagonizes cyclic AMP-cyclic AMP receptor protein activation of the deoCp2 promoter of Escherichia coli K-12." J Bacteriol 1990;172(10);5706-13. PMID: 2170326

SogaardAndersen90a: Sogaard-Andersen L, Mollegaard NE, Douthwaite SR, Valentin-Hansen P (1990). "Tandem DNA-bound cAMP-CRP complexes are required for transcriptional repression of the deoP2 promoter by the CytR repressor in Escherichia coli." Mol Microbiol 4(9);1595-601. PMID: 1962841

SogaardAndersen91b: Sogaard-Andersen L, Pedersen H, Holst B, Valentin-Hansen P (1991). "A novel function of the cAMP-CRP complex in Escherichia coli: cAMP-CRP functions as an adaptor for the CytR repressor in the deo operon." Mol Microbiol 5(4);969-75. PMID: 1649947

ValentinHansen96: Valentin-Hansen P, Sogaard-Andersen L, Pedersen H (1996). "A flexible partnership: the CytR anti-activator and the cAMP-CRP activator protein, comrades in transcription control." Mol Microbiol 20(3);461-6. PMID: 8736525

Yamamoto05b: Yamamoto K, Ishihama A (2005). "Transcriptional response of Escherichia coli to external zinc." J Bacteriol 187(18);6333-40. PMID: 16159766

Yura93: Yura T, Nagai H, Mori H (1993). "Regulation of the heat-shock response in bacteria." Annu Rev Microbiol 47;321-50. PMID: 7504905

Zahrl06: Zahrl D, Wagner M, Bischof K, Koraimann G (2006). "Expression and assembly of a functional type IV secretion system elicit extracytoplasmic and cytoplasmic stress responses in Escherichia coli." J Bacteriol 188(18);6611-21. PMID: 16952953

Zheng04: Zheng D, Constantinidou C, Hobman JL, Minchin SD (2004). "Identification of the CRP regulon using in vitro and in vivo transcriptional profiling." Nucleic Acids Res 32(19);5874-93. PMID: 15520470

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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