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Escherichia coli K-12 substr. MG1655 Polypeptide: dynamic cytoskeletal protein MreB



Gene: mreB Accession Numbers: EG10608 (EcoCyc), b3251, ECK3239

Synonyms: rodY, envB, mon, mreB_1

Regulation Summary Diagram: ?

Regulation summary diagram for mreB

Summary:
MreB is a homologue of the eukaryotic actin protein (see [Bork92, vandenEnt01].

MreB is implicated in the formation of rod shape and mecillinam sensitivity [Doi88]. MreB forms left-handed helical filaments beneath the surface of the cell [Kruse03, Shih03, Wang12]. MreB helical filaments are artifacts of the yellow fluorescent tag used for imaging; MreB helical filaments do not form when the tag is removed and cells expressing a MreB-mCherry fusion protein do not contain helical filaments [Swulius12]. MreB forms dynamic filaments up to 1.5 µm in length [Reimold13].

Cells depleted of MreB become spherical and eventually lyse; MreB interacts with itself and with MreC; MreB localisation is disrupted in cells depleted in MrdB, MreC or MreD (all of which have a spherical shape) [Kruse05]. Under slow growth conditions, cells lacking MreB grow and divide as small spheres; under fast growth conditions they form giant non-dividing and non-propagating spheres; spherical cell defects can be rescued by overexpression of ftsZ [Bendezu08].

MreB is a dynamic cytoskeletal protein - it persistantly rotates around the long axis of the cell; MreB motion is blocked in strains that cannot synthesise the essential peptidoglycan component - diaminopimelic acid, and by antibiotics that inhibit cell wall synthesis [vanTeeffelen11]. MreB localisation occurs in a curve dependent manner - MreB is enriched at negatively curved regions of the cell wall and depleted at positively curved regions. Cell wall growth is colocalised with MreB which results in bursts of localised growth [Ursell14].

MreB interacts directly with the inner membrane via a predicted N-terminal amphipathic helix; this interaction is required for cell shape maintenance and viability [Salje11]. MreB interacts with RodZ and this interaction is required for maintenance of cell shape [Bendezu09].

MreB is implicated in chromosome segregation [Kruse03]. MreB is required for segregation of the origin of replication (oriC); MreB interacts with RNA polymerase in vivo and in vitro [Kruse06]. MreB interacts with topoisomerase IV likely via its ParC subunit and regulates its activity in vitro; ΔmreB mutants are deficient in Topo IV activity [Madabhushi09]. MreB is not involved in chromosome segregation [Karczmarek07].

The MreB cytoskeleton duplicates and segregates before the completion of cytokinesis; transverse MreB ring structures, located near the midcell are intermediates in this process [Vats07]. The ring structures contain MreB, MreC, MreD, MrdB and MrdA; assembly of these proteins is dependent on the presence of the FtsZ ring [Vats09]. MreB appears in a punctate pattern along the cell periphery and forms ring-like structures at mid-cell in cells undergoing division; MreB is recruited to the Z-ring; MreB interacts with FtsZ in vivo and this interaction functions to deliver MrcA and MrdA to the Z ring [Fenton13].

MreB interacts with SetB [Espeli03].

MreB is the target of the antibacterial compound A22 [S-(3,4-dichlorobenzyl)isothiourea] [Kruse06]

MreB interacts with the T7 bacteriophage encoded growth inhibitor Gp0.6 [MolshanskiMor14]

mreB, mreC and mreD from an operon in E. coli K-12, largely transcribed as monocistronic mreB mRNA [Wachi06]

Reviews: [Kruse05a, White12]
Comment: [Margolin12]

Citations: [Wachi87, Wachi89, Freire09, Iwai02, Varma09, Shih05, Nilsen05, Swulius11]

Locations: inner membrane, cytoskeleton

Map Position: [3,398,066 <- 3,399,109] (73.24 centisomes, 264°)
Length: 1044 bp / 347 aa

Molecular Weight of Polypeptide: 36.952 kD (from nucleotide sequence), 37.0 kD (experimental) [Doi88 ]

Unification Links: ASAP:ABE-0010661 , CGSC:31343 , DIP:DIP-31874N , EchoBASE:EB0603 , EcoGene:EG10608 , EcoliWiki:b3251 , Mint:MINT-1222190 , ModBase:P0A9X4 , OU-Microarray:b3251 , PortEco:mreB , PR:PRO_000023289 , Pride:P0A9X4 , Protein Model Portal:P0A9X4 , RefSeq:NP_417717 , RegulonDB:EG10608 , SMR:P0A9X4 , String:511145.b3251 , Swiss-Model:P0A9X4 , UniProt:P0A9X4

Relationship Links: InterPro:IN-FAMILY:IPR004753 , Pfam:IN-FAMILY:PF06723 , Prints:IN-FAMILY:PR01652

In Paralogous Gene Group: 5 (5 members) , 510 (2 members)

GO Terms:

Biological Process: GO:0008360 - regulation of cell shape Inferred from experiment Inferred by computational analysis [UniProtGOA11, Kruse05, Bendezu08]
GO:0043093 - FtsZ-dependent cytokinesis Inferred from experiment [Fenton13]
GO:0051782 - negative regulation of cell division Inferred from experiment [Wachi89a]
GO:0051983 - regulation of chromosome segregation Inferred from experiment [Kruse06, Madabhushi09, Kruse03]
GO:0000902 - cell morphogenesis Inferred by computational analysis [GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Bendezu09, Madabhushi09, Espeli03, Fenton13, Butland05, Masuda12, Kruse05]
GO:0042802 - identical protein binding Inferred from experiment [Kruse05, Fenton13, Masuda12]
Cellular Component: GO:0005856 - cytoskeleton Inferred from experiment [Shih03, Kruse03, Vats09]
GO:0005886 - plasma membrane Inferred from experiment [Kruse05]
GO:0031226 - intrinsic component of plasma membrane Inferred from experiment [Salje11]

MultiFun Terms: cell processes cell division
cell processes protection drug resistance/sensitivity

Essentiality data for mreB knockouts: ?

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

Credits:
Revised 26-May-2015 by Mackie A , Macquarie University
Last-Curated ? 26-May-2015 by Mackie A , Macquarie University


Sequence Features

Protein sequence of dynamic cytoskeletal protein MreB with features indicated

Feature Class Location Common Name Citations Comment
Protein-Structure-Region 3 -> 8 amphipathic helix
[Salje11, Salje11]
predicted amphipathic helix that is required for membrane interaction
Conserved-Region 12 -> 34 Phosphate 1
[Bork92]
conserved motif in the actin family
Sequence-Conflict 60 -> 61  
[Doi88, UniProt10]
UniProt: (in Ref. 1; AAA83891);
Conserved-Region 135 -> 154 Connect 1
[Bork92]
conserved motif in the actin family
Conserved-Region 161 -> 181 Phosphate 2
[Bork92]
conserved motif in the actin family
Mutagenesis-Variant 165  
[Kruse03]
mutation of this residue to V, E or A interferes with MreB filament formation and cell division, cells retain their rod shape
Sequence-Conflict 265  
[Doi88, UniProt10]
UniProt: (in Ref. 1; AAA83891);
Sequence-Conflict 277 -> 278  
[Doi88, UniProt10]
UniProt: (in Ref. 1; AAA83891);
Mutagenesis-Variant 285  
[Fenton13]
alternate sequence D → A: reduced recruitment of mutant to the Z-ring and inhibited cell division
Mutagenesis-Variant 288  
[MolshanskiMor14]
alternate sequence E →G renders cell resistant to the T7 bacteriophage growth inhibitor Gp0.6
Conserved-Region 288 -> 307 Adenosine
[Bork92]
conserved motif in the actin family
Conserved-Region 318 -> 338 Connect 2
[Bork92]
conserved motif of the actin family


Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Notes:

History:
Peter D. Karp on Wed Jan 18, 2006:
Gene right-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
3/2/1998 (pkarp) Merged genes G454/b3251 and EG10608/mreB
10/20/97 Gene b3251 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10608; confirmed by SwissProt match.


References

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

Bendezu08: Bendezu FO, de Boer PA (2008). "Conditional lethality, division defects, membrane involution, and endocytosis in mre and mrd shape mutants of Escherichia coli." J Bacteriol 190(5);1792-811. PMID: 17993535

Bendezu09: Bendezu FO, Hale CA, Bernhardt TG, de Boer PA (2009). "RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. coli." EMBO J 28(3);193-204. PMID: 19078962

Bork92: Bork P, Sander C, Valencia A (1992). "An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins." Proc Natl Acad Sci U S A 89(16);7290-4. PMID: 1323828

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Doi88: Doi M, Wachi M, Ishino F, Tomioka S, Ito M, Sakagami Y, Suzuki A, Matsuhashi M (1988). "Determinations of the DNA sequence of the mreB gene and of the gene products of the mre region that function in formation of the rod shape of Escherichia coli cells." J Bacteriol 170(10);4619-24. PMID: 3049542

Espeli03: Espeli O, Nurse P, Levine C, Lee C, Marians KJ (2003). "SetB: an integral membrane protein that affects chromosome segregation in Escherichia coli." Mol Microbiol 50(2);495-509. PMID: 14617174

Fenton13: Fenton AK, Gerdes K (2013). "Direct interaction of FtsZ and MreB is required for septum synthesis and cell division in Escherichia coli." EMBO J 32(13);1953-65. PMID: 23756461

Freire09: Freire P, Moreira RN, Arraiano CM (2009). "BolA inhibits cell elongation and regulates MreB expression levels." J Mol Biol 385(5);1345-51. PMID: 19111750

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

Iwai02: Iwai N, Nagai K, Wachi M (2002). "Novel S-benzylisothiourea compound that induces spherical cells in Escherichia coli probably by acting on a rod-shape-determining protein(s) other than penicillin-binding protein 2." Biosci Biotechnol Biochem 66(12);2658-62. PMID: 12596863

Karczmarek07: Karczmarek A, Martinez-Arteaga R, Baselga RM, Alexeeva S, Hansen FG, Vicente M, Nanninga N, den Blaauwen T (2007). "DNA and origin region segregation are not affected by the transition from rod to sphere after inhibition of Escherichia coli MreB by A22." Mol Microbiol 65(1);51-63. PMID: 17581120

Kruse03: Kruse T, Moller-Jensen J, Lobner-Olesen A, Gerdes K (2003). "Dysfunctional MreB inhibits chromosome segregation in Escherichia coli." EMBO J 22(19);5283-92. PMID: 14517265

Kruse05: Kruse T, Bork-Jensen J, Gerdes K (2005). "The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex." Mol Microbiol 55(1);78-89. PMID: 15612918

Kruse05a: Kruse T, Gerdes K (2005). "Bacterial DNA segregation by the actin-like MreB protein." Trends Cell Biol 15(7);343-5. PMID: 15922599

Kruse06: Kruse T, Blagoev B, Lobner-Olesen A, Wachi M, Sasaki K, Iwai N, Mann M, Gerdes K (2006). "Actin homolog MreB and RNA polymerase interact and are both required for chromosome segregation in Escherichia coli." Genes Dev 20(1);113-24. PMID: 16391237

Madabhushi09: Madabhushi R, Marians KJ (2009). "Actin homolog MreB affects chromosome segregation by regulating topoisomerase IV in Escherichia coli." Mol Cell 33(2);171-80. PMID: 19187760

Margolin12: Margolin W (2012). "The price of tags in protein localization studies." J Bacteriol 194(23);6369-71. PMID: 22961859

Masuda12: Masuda H, Tan Q, Awano N, Wu KP, Inouye M (2012). "YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ, antagonizing the CbtA (YeeV) toxicity in Escherichia coli." Mol Microbiol 84(5);979-89. PMID: 22515815

MolshanskiMor14: Molshanski-Mor S, Yosef I, Kiro R, Edgar R, Manor M, Gershovits M, Laserson M, Pupko T, Qimron U (2014). "Revealing bacterial targets of growth inhibitors encoded by bacteriophage T7." Proc Natl Acad Sci U S A 111(52);18715-20. PMID: 25512533

Nilsen05: Nilsen T, Yan AW, Gale G, Goldberg MB (2005). "Presence of multiple sites containing polar material in spherical Escherichia coli cells that lack MreB." J Bacteriol 187(17);6187-96. PMID: 16109960

Reimold13: Reimold C, Defeu Soufo HJ, Dempwolff F, Graumann PL (2013). "Motion of variable-length MreB filaments at the bacterial cell membrane influences cell morphology." Mol Biol Cell 24(15);2340-9. PMID: 23783036

Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293

Salje11: Salje J, van den Ent F, de Boer P, Lowe J (2011). "Direct membrane binding by bacterial actin MreB." Mol Cell 43(3);478-87. PMID: 21816350

Shih03: Shih YL, Le T, Rothfield L (2003). "Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles." Proc Natl Acad Sci U S A 100(13);7865-70. PMID: 12766229

Shih05: Shih YL, Kawagishi I, Rothfield L (2005). "The MreB and Min cytoskeletal-like systems play independent roles in prokaryotic polar differentiation." Mol Microbiol 58(4);917-28. PMID: 16262780

Swulius11: Swulius MT, Chen S, Jane Ding H, Li Z, Briegel A, Pilhofer M, Tocheva EI, Lybarger SR, Johnson TL, Sandkvist M, Jensen GJ (2011). "Long helical filaments are not seen encircling cells in electron cryotomograms of rod-shaped bacteria." Biochem Biophys Res Commun 407(4);650-5. PMID: 21419100

Swulius12: Swulius MT, Jensen GJ (2012). "The helical MreB cytoskeleton in Escherichia coli MC1000/pLE7 is an artifact of the N-Terminal yellow fluorescent protein tag." J Bacteriol 194(23);6382-6. PMID: 22904287

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Ursell14: Ursell TS, Nguyen J, Monds RD, Colavin A, Billings G, Ouzounov N, Gitai Z, Shaevitz JW, Huang KC (2014). "Rod-like bacterial shape is maintained by feedback between cell curvature and cytoskeletal localization." Proc Natl Acad Sci U S A 111(11);E1025-34. PMID: 24550515

vandenEnt01: van den Ent F, Amos L, Lowe J (2001). "Bacterial ancestry of actin and tubulin." Curr Opin Microbiol 4(6);634-8. PMID: 11731313

vanTeeffelen11: van Teeffelen S, Wang S, Furchtgott L, Huang KC, Wingreen NS, Shaevitz JW, Gitai Z (2011). "The bacterial actin MreB rotates, and rotation depends on cell-wall assembly." Proc Natl Acad Sci U S A 108(38);15822-7. PMID: 21903929

Varma09: Varma A, Young KD (2009). "In Escherichia coli, MreB and FtsZ direct the synthesis of lateral cell wall via independent pathways that require PBP 2." J Bacteriol 191(11);3526-33. PMID: 19346310

Vats07: Vats P, Rothfield L (2007). "Duplication and segregation of the actin (MreB) cytoskeleton during the prokaryotic cell cycle." Proc Natl Acad Sci U S A 104(45);17795-800. PMID: 17978175

Vats09: Vats P, Shih YL, Rothfield L (2009). "Assembly of the MreB-associated cytoskeletal ring of Escherichia coli." Mol Microbiol 72(1);170-82. PMID: 19220747

Wachi06: Wachi M, Osaka K, Kohama T, Sasaki K, Ohtsu I, Iwai N, Takada A, Nagai K (2006). "Transcriptional analysis of the Escherichia coli mreBCD genes responsible for morphogenesis and chromosome segregation." Biosci Biotechnol Biochem 70(11);2712-9. PMID: 17090951

Wachi87: Wachi M, Doi M, Tamaki S, Park W, Nakajima-Iijima S, Matsuhashi M (1987). "Mutant isolation and molecular cloning of mre genes, which determine cell shape, sensitivity to mecillinam, and amount of penicillin-binding proteins in Escherichia coli." J Bacteriol 169(11);4935-40. PMID: 2822655

Wachi89: Wachi M, Doi M, Okada Y, Matsuhashi M (1989). "New mre genes mreC and mreD, responsible for formation of the rod shape of Escherichia coli cells." J Bacteriol 171(12);6511-6. PMID: 2687239

Wachi89a: Wachi M, Matsuhashi M (1989). "Negative control of cell division by mreB, a gene that functions in determining the rod shape of Escherichia coli cells." J Bacteriol 171(6);3123-7. PMID: 2656641

Wang12: Wang S, Furchtgott L, Huang KC, Shaevitz JW (2012). "Helical insertion of peptidoglycan produces chiral ordering of the bacterial cell wall." Proc Natl Acad Sci U S A 109(10);E595-604. PMID: 22343529

White12: White CL, Gober JW (2012). "MreB: pilot or passenger of cell wall synthesis?." Trends Microbiol 20(2);74-9. PMID: 22154164

Other References Related to Gene Regulation

Pruss01: Pruss BM, Liu X, Hendrickson W, Matsumura P (2001). "FlhD/FlhC-regulated promoters analyzed by gene array and lacZ gene fusions." FEMS Microbiol Lett 2001;197(1);91-7. PMID: 11287152

Wachi91: Wachi M, Doi M, Ueda T, Ueki M, Tsuritani K, Nagai K, Matsuhashi M (1991). "Sequence of the downstream flanking region of the shape-determining genes mreBCD of Escherichia coli." Gene 1991;106(1);135-6. PMID: 1937035


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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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