A family of related ATP-binding subunits coupled to many distinct biological processes in bacteria
- PMID: 3762694
- DOI: 10.1038/323448a0
A family of related ATP-binding subunits coupled to many distinct biological processes in bacteria
Abstract
Many biological processes are coupled to ATP hydrolysis. We describe here a class of closely related ATP-binding proteins, from several bacterial species, which are associated with a variety of cellular functions including membrane transport, cell division, nodulation in Rhizobium and haemolysin export. These proteins comprise a family of structurally and functionally related subunits which share a common evolutionary origin, bind ATP and probably serve to couple ATP hydrolysis to each of these biological processes. This finding suggests a specific role for ATP in cell division, nodulation during nitrogen fixation and protein export, and allows us to assign a probable function to one of the protein components from each of these systems.
Similar articles
-
Sequence relationships between integral inner membrane proteins of binding protein-dependent transport systems: evolution by recurrent gene duplications.Protein Sci. 1994 Feb;3(2):325-44. doi: 10.1002/pro.5560030216. Protein Sci. 1994. PMID: 8003968 Free PMC article.
-
The homologous pairing domain of RecA also mediates the allosteric regulation of DNA binding and ATP hydrolysis: a remarkable concentration of functional residues.J Mol Biol. 2000 Nov 10;303(5):709-20. doi: 10.1006/jmbi.2000.4163. J Mol Biol. 2000. PMID: 11061970
-
Mechanisms of type III protein export for bacterial flagellar assembly.Mol Biosyst. 2008 Nov;4(11):1105-15. doi: 10.1039/b808065h. Epub 2008 Sep 24. Mol Biosyst. 2008. PMID: 18931786 Review.
-
A family of closely related ATP-binding subunits from prokaryotic and eukaryotic cells.Bioessays. 1988 Apr;8(4):111-6. doi: 10.1002/bies.950080406. Bioessays. 1988. PMID: 3288195 Review. No abstract available.
-
Modulator-induced interference in functional cross talk between the substrate and the ATP sites of human P-glycoprotein.Biochemistry. 2006 Feb 28;45(8):2739-51. doi: 10.1021/bi0521745. Biochemistry. 2006. PMID: 16489767
Cited by
-
Topological and functional studies on HlyB of Escherichia coli.Mol Gen Genet. 1992 Mar;232(1):40-8. doi: 10.1007/BF00299135. Mol Gen Genet. 1992. PMID: 1552901
-
Amplification of bacterial genomic DNA by the polymerase chain reaction and direct sequencing after asymmetric amplification: application to the study of periplasmic permeases.J Bacteriol. 1989 Mar;171(3):1602-8. doi: 10.1128/jb.171.3.1602-1608.1989. J Bacteriol. 1989. PMID: 2646290 Free PMC article.
-
Protease secretion by Erwinia chrysanthemi: the specific secretion functions are analogous to those of Escherichia coli alpha-haemolysin.EMBO J. 1990 May;9(5):1375-82. doi: 10.1002/j.1460-2075.1990.tb08252.x. EMBO J. 1990. PMID: 2184029 Free PMC article.
-
The antigen 85 complex: a major secretion product of Mycobacterium tuberculosis.Microbiol Rev. 1992 Dec;56(4):648-61. doi: 10.1128/mr.56.4.648-661.1992. Microbiol Rev. 1992. PMID: 1480113 Free PMC article. Review.
-
Secretion of hybrid proteins by the Yersinia Yop export system.J Bacteriol. 1991 Mar;173(5):1677-85. doi: 10.1128/jb.173.5.1677-1685.1991. J Bacteriol. 1991. PMID: 1999387 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
