|Gene:||zapA||Accession Numbers: EG12878 (EcoCyc), b2910, ECK2905|
ZapA binds to FtsZ polymers [Small07] and promotes the coherence of the Z-ring by cross-linking FtsZ polymers and stabilizing longitudinal interactions between FtsZ molecules [Dajkovic10]. This effect is counteracted by ZapB [Galli12].
Before septum formation, a complex of the early-division proteins ZipA, ZapA, and ZapB oscillates along the cell with a periodicity that is opposite that of MinC. The oscillation is dependent on the presence of FtsZ filaments and on the Min system [Bisicchia13].
During growth in minimal medium, ZapA and FtsZ are present at approximately equimolar concentration [Mohammadi09]. ZapA was reported to be a potent inhibitor of the GTPase activity of FtsZ [Small07], but later experiments with ZapA lacking a His tag found little effect of ZapA on FtsZ GTPase activity [Mohammadi09]. [Galli12] found that inhibition of the GTPase activity of FtsZ by ZapA was stronger at pH 6.5 than at pH 7.5; at the higher pH, addition of ZapB further weakened the effect.
ZapA localizes to the cell division site, but is not essential [GueirosFilho02]. It is not required for targeting of the MinC/MinD complex to the Z-ring [Johnson04a], but is required for recruiting ZapB to the Z-ring [Galli10]. ZapA also interacts with FtsI and FtsN [Alexeeva10] and indirectly, via FtsZ, with ZipA [Pazos13]. FtsZ and ZapA disassemble from the cell division site before the constriction of the inner membrane is complete and the cytoplasm is separated [Soderstrom14].
A preliminary analysis of the crystal structure of ZapA has been published [Addinall05], and a crystal structure has been solved at 1.95 Å resolution [Roach14]. ZapA consists of two domains; the N-terminal globular domain is required for interaction with FtsZ, while the C-terminal coiled-coil domain is required for interaction with ZapB and for homodimerization [Galli12]. ZapA exists in a dimer/tetramer equilibrium in solution [Small07]. An I83E mutant is a constitutive dimer that is able to bind to FtsZ, but is unable to induce FtsZ bundling [PachecoGomez13]. Residues that are involved in the interaction with FtsZ and in filament bundling were identified by site-directed mutagenesis [Roach14].
A zapA deletion strain has a cytokinesis defect [Mohammadi09, Dajkovic10, Buss13]. Reports disagree on whether [Dajkovic10] or not [Mohammadi09] His-tagged ZapA can complement the defect. A zapA mutant has an abnormal cell division septum; single-molecule based superresolution imaging shows a disordered arrangement of FtsZ clusters [Buss13]. Overproduction of ZapA results in aberrant localization of FtsZ and ZapB and the formation of elongated cells [Galli12].
ZapA: "Z-ring-associated protein A" [GueirosFilho02]
Locations: inner membrane, cytosol
|Map Position: [3,053,634 -> 3,053,963] (65.82 centisomes, 237°)||Length: 330 bp / 109 aa|
Molecular Weight of Polypeptide: 12.594 kD (from nucleotide sequence)
Unification Links: ASAP:ABE-0009554 , EchoBASE:EB2716 , EcoGene:EG12878 , EcoliWiki:b2910 , ModBase:P0ADS2 , OU-Microarray:b2910 , PortEco:zapA , PR:PRO_000024245 , Pride:P0ADS2 , Protein Model Portal:P0ADS2 , RefSeq:NP_417386 , RegulonDB:EG12878 , SMR:P0ADS2 , String:511145.b2910 , UniProt:P0ADS2
|Biological Process:||GO:0000917 - barrier septum assembly
[UniProtGOA11a, GOA06, Galli10]
GO:0000921 - septin ring assembly [Goehring05]
GO:0043093 - FtsZ-dependent cytokinesis [Dajkovic10, Mohammadi09]
GO:0051301 - cell division [UniProtGOA11a, GOA06, Galli10, Small07]
GO:0007049 - cell cycle [UniProtGOA11a]
|Molecular Function:||GO:0005515 - protein binding
[Galli12, Alexeeva10, Small07, Galli10]
GO:0042802 - identical protein binding [Alexeeva10]
|Cellular Component:||GO:0005829 - cytosol
GO:0030428 - cell septum [Galli10]
GO:0032153 - cell division site [Goehring05]
GO:0005737 - cytoplasm [UniProtGOA11, UniProtGOA11a]
GO:0005886 - plasma membrane [GOA06]
|MultiFun Terms:||cell processes → cell division|
|Growth Medium||Growth?||T (°C)||O2||pH||Osm/L||Growth Observations|
|LB enriched||Yes||37||Aerobic||6.95||Yes [Gerdes03, Comment 1]|
|LB Lennox||Yes||37||Aerobic||7||Yes [Baba06, Comment 2]|
|M9 medium with 1% glycerol||Yes||37||Aerobic||7.2||0.35||Yes [Joyce06, Comment 3]|
|MOPS medium with 0.4% glucose||Yes||37||Aerobic||7.2||0.22||Yes [Baba06, Comment 2]|
Peter D. Karp on Thu Jan 16, 2003:
Predicted gene function revised as a result of E. coli genome reannotation by Serres et al. [Serres01 ].
10/20/97 Gene b2910 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG12878; confirmed by SwissProt match.
Abe13: Abe A, Furukawa S, Migita Y, Tanaka M, Ogihara H, Morinaga Y (2013). "Sublethal high hydrostatic pressure treatment reveals the importance of genes coding cytoskeletal protein in Escherichia coli morphogenesis." Curr Microbiol 67(5);515-21. PMID: 23708427
Addinall05: Addinall SG, Johnson KA, Dafforn T, Smith C, Rodger A, Gomez RP, Sloan K, Blewett A, Scott DJ, Roper DI (2005). "Expression, purification and crystallization of the cell-division protein YgfE from Escherichia coli." Acta Crystallograph Sect F Struct Biol Cryst Commun 61(Pt 3);305-7. PMID: 16511026
Alexeeva10: Alexeeva S, Gadella TW, Verheul J, Verhoeven GS, den Blaauwen T (2010). "Direct interactions of early and late assembling division proteins in Escherichia coli cells resolved by FRET." Mol Microbiol 77(2);384-98. PMID: 20497333
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
Bisicchia13: Bisicchia P, Arumugam S, Schwille P, Sherratt D (2013). "MinC, MinD, and MinE drive counter-oscillation of early-cell-division proteins prior to Escherichia coli septum formation." MBio 4(6);e00856-13. PMID: 24327341
Buss13: Buss J, Coltharp C, Huang T, Pohlmeyer C, Wang SC, Hatem C, Xiao J (2013). "In vivo organization of the FtsZ-ring by ZapA and ZapB revealed by quantitative super-resolution microscopy." Mol Microbiol 89(6);1099-120. PMID: 23859153
Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938
Goehring05: Goehring NW, Gueiros-Filho F, Beckwith J (2005). "Premature targeting of a cell division protein to midcell allows dissection of divisome assembly in Escherichia coli." Genes Dev 19(1);127-37. PMID: 15630023
GueirosFilho02: Gueiros-Filho FJ, Losick R (2002). "A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ." Genes Dev 16(19);2544-56. PMID: 12368265
Johnson04a: Johnson JE, Lackner LL, Hale CA, de Boer PA (2004). "ZipA is required for targeting of DMinC/DicB, but not DMinC/MinD, complexes to septal ring assemblies in Escherichia coli." J Bacteriol 186(8);2418-29. PMID: 15060045
Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394
Mohammadi09: Mohammadi T, Ploeger GE, Verheul J, Comvalius AD, Martos A, Alfonso C, van Marle J, Rivas G, den Blaauwen T (2009). "The GTPase activity of Escherichia coli FtsZ determines the magnitude of the FtsZ polymer bundling by ZapA in vitro." Biochemistry 48(46);11056-66. PMID: 19842714
Nakahigashi92: Nakahigashi K, Miyamoto K, Nishimura K, Inokuchi H (1992). "Isolation and characterization of a light-sensitive mutant of Escherichia coli K-12 with a mutation in a gene that is required for the biosynthesis of ubiquinone." J Bacteriol 1992;174(22);7352-9. PMID: 1339425
PachecoGomez13: Pacheco-Gomez R, Cheng X, Hicks MR, Smith CJ, Roper DI, Addinall S, Rodger A, Dafforn TR (2013). "Tetramerization of ZapA is required for FtsZ bundling." Biochem J 449(3);795-802. PMID: 23098212
Pazos13: Pazos M, Natale P, Margolin W, Vicente M (2013). "Interactions among the early Escherichia coli divisome proteins revealed by bimolecular fluorescence complementation." Environ Microbiol 15(12);3282-91. PMID: 23957637
Roach14: Roach EJ, Kimber MS, Khursigara CM (2014). "Crystal structure and site-directed mutational analysis reveals key residues involved in Escherichia coli ZapA function." J Biol Chem. PMID: 25002581
Small07: Small E, Marrington R, Rodger A, Scott DJ, Sloan K, Roper D, Dafforn TR, Addinall SG (2007). "FtsZ Polymer-bundling by the Escherichia coli ZapA Orthologue, YgfE, Involves a Conformational Change in Bound GTP." J Mol Biol 369(1):210-21. PMID: 17428494
Soderstrom14: Soderstrom B, Skoog K, Blom H, Weiss DS, von Heijne G, Daley DO (2014). "Disassembly of the divisome in Escherichia coli: evidence that FtsZ dissociates before compartmentalization." Mol Microbiol 92(1);1-9. PMID: 24506818
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