Escherichia coli K-12 substr. MG1655 Polypeptide: MreB

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

Synonyms: rodY, envB, mon, mreB_1

Regulation Summary Diagram: ?

Regulation summary diagram for mreB

Component of: longitudinal peptidoglycan synthesis/chromosome segregation-directing complex (extended summary available)

BolA represses mreB transcription [Freire09].

Gene Citations: [Wachi06]

Locations: 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)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0008360 - regulation of cell shape Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Wachi87, Bendezu08]
GO:0051782 - negative regulation of cell division Inferred from experiment [Wachi89]
GO:0051983 - regulation of chromosome segregation Inferred from experiment [Madabhushi09, Kruse03]
GO:0000902 - cell morphogenesis Inferred by computational analysis [GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Fenton13, Butland05, Masuda12a, Kruse05]
GO:0042802 - identical protein binding Inferred from experiment [Fenton13, Masuda12a]
Cellular Component: GO:0005856 - cytoskeleton Inferred from experiment [Vats09]

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]

Subunit of: longitudinal peptidoglycan synthesis/chromosome segregation-directing complex

Subunit composition of longitudinal peptidoglycan synthesis/chromosome segregation-directing complex = [MreB][MreC][MreD]

The mre genes are responsible for rod shape and mecillinam sensitivity in E. coli [Wachi87, Wachi89a]. Fluorescence microscopy has shown that MreB, an actin homolog, forms left-handed helical filaments beneath the surface of the cell [Kruse03, Shih03, Wang12i]. Filament formation has been shown to be dependent upon the rod-shape of the cell [Kruse05]. MreB is also incorporated into cytoskeletal rings that are located near the midcell during cell division [Vats07].

MreB is responsible for proper chromosome segregation and movement. Overexpression of MreB inhibits cell division. Overexpression of dysfunctional MreB results in altered MreB filament morphology, inhibition of cell division, mislocalized origin and terminus regions of the chromosome, and perturbed DNA segregation [Kruse03]. Deletion of mreB results in spherical cell shape and eventual lysis [Bendezu08].

SetB is involved in protein segregation and likely acts somewhere in the linkage of chromosomes to the force required to separate them [Espeli03]. Co-expression of SetB-GFP and Myc-MreB showed that the two proteins co-localized and yeast two-hybrid experiments revealed that SetB and MreB interact.

Overexpression of ftsQAZ suppresses the lethality of MreBCD depletion by increasing the supply of monomers for the enlarged Z ring of round cells during division. Fractionation and GFP fusions studies have shown MreC and MreD associate with the inner membrane. Two-hybrid experiments have shown that MreBCD form a complex in which MreB interacts with itself and MreC, and MreC interacts with itself and MreD.

The coiled-coil domain of MreC is believed to allow it to dimerize while its alpha helices are embedded within the inner membrane. MreD is predicted to be membrane bound with five transmembrane α-helices. The cytoplasmic 13 -14 N-terminal amino acids of MreC are believed to interact with MreB lying just beneath the cell surface. MreC is also believed to interact with PBP2, which is responsible for lateral wall peptidoglycan synthesis, suggesting a role for the MreBCD complex in directing peptidoglycan formation through this interaction [Kruse05]. Immunofluorescence microscopy has shown PBP2 localization in the cell periphery in band-like structures is similar to MreB localization and is dependent upon MreB in Caulobacter crescentus [Figge04] and E.coli [Vats09]. Immunofluorescence microscopy has also shown that assembly of MreB, MreC and MreD into the cytoskeletal rings and coiled structures occurs independently [Vats09].

MreB is a dynamic cytoskeletal protein - it persistantly rotates around the long axis of the cell [vanTeeffelen11]. 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, mreC and mreD from an operon in E. coli K-12, largely transcribed as monocistronic mreB mRNA. mreB, mreC and mreD are all essential in E. coli [Wachi06]

Reviews: [CarballidoLopez06, Kruse05a, Shaevitz10].

Citations: [Pradel09, White12]

Locations: cytoskeleton

GO Terms:

Biological Process: GO:0008360 - regulation of cell shape Inferred from experiment [Wachi89a, Wachi87]
Cellular Component: GO:0005856 - cytoskeleton Inferred from experiment [Shih03]

Sequence Features

Protein sequence of MreB with features indicated

Feature Class Location Citations Comment
Sequence-Conflict 60 -> 61
[Doi88, UniProt10a]
UniProt: (in Ref. 1; AAA83891);
Sequence-Conflict 265
[Doi88, UniProt10a]
UniProt: (in Ref. 1; AAA83891);
Sequence-Conflict 277 -> 278
[Doi88, UniProt10a]
UniProt: (in Ref. 1; AAA83891);

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


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.


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

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

CarballidoLopez06: Carballido-Lopez R (2006). "The bacterial actin-like cytoskeleton." Microbiol Mol Biol Rev 70(4);888-909. PMID: 17158703

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

Figge04: Figge RM, Divakaruni AV, Gober JW (2004). "MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus." Mol Microbiol 51(5);1321-32. PMID: 14982627

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

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

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

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

Masuda12a: 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

Pradel09: Pradel N, Delmas J, Wu LF, Santini CL, Bonnet R (2009). "Sec- and Tat-dependent translocation of beta-lactamases across the Escherichia coli inner membrane." Antimicrob Agents Chemother 53(1);242-8. PMID: 18981261

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

Shaevitz10: Shaevitz JW, Gitai Z (2010). "The structure and function of bacterial actin homologs." Cold Spring Harb Perspect Biol 2(9);a000364. PMID: 20630996

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

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProtGOA11a: 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

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

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, 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

Wachi89a: 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

Wang12i: 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
Page generated by SRI International Pathway Tools version 19.0 on Wed May 27, 2015, BIOCYC13A.