|Gene:||mreB||Accession Numbers: EG10608 (EcoCyc), b3251, ECK3239|
Synonyms: rodY, envB, mon, mreB_1
Component of: longitudinal peptidoglycan synthesis/chromosome segregation-directing complex (extended summary available)
BolA represses mreB transcription [Freire09].
Gene Citations: [Wachi06]
|Map Position: [3,398,066 <- 3,399,109] (73.24 centisomes)||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
|Biological Process:||GO:0008360 - regulation of cell shape
[UniProtGOA11a, Wachi87, Bendezu08]
GO:0051782 - negative regulation of cell division [Wachi89]
GO:0051983 - regulation of chromosome segregation [Madabhushi09, Kruse03]
GO:0000902 - cell morphogenesis [GOA01a]
|Molecular Function:||GO:0005515 - protein binding
[Fenton13, Butland05, Masuda12, Kruse05]
GO:0042802 - identical protein binding [Fenton13, Masuda12]
|Cellular Component:||GO:0005856 - cytoskeleton [Vats09]|
|MultiFun Terms:||cell processes → cell division|
|cell processes → protection → drug resistance/sensitivity|
|Growth Medium||Growth?||T (°C)||O2||pH||Osm/L||Growth Observations|
|LB Lennox||No||37||Aerobic||7||No [Baba06, Comment 1]|
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, Wang12e]. 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]
|Biological Process:||GO:0008360 - regulation of cell shape [Wachi89a, Wachi87]|
|Cellular Component:||GO:0005856 - cytoskeleton [Shih03]|
|Sequence-Conflict||60 -> 61|
|Sequence-Conflict||277 -> 278|
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
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
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
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
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
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
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
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
Wang12e: 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
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
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493