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Cell division protein FtsA, predicted to belong to the actin family, is present in different cell compartments depending on its phosphorylation state. The FtsA fraction isolated from the cytoplasm is phosphorylated and capable of binding ATP, while the membrane-bound form is unphosphorylated and does not bind ATP. A variant of the protein FtsA102, in which the nucleotide binding site was destroyed by mutagenesis of a highly conserved residue predicted to be needed for the binding, does not bind ATP. Another variant, FtsA104, cannot be phosphorylated because the predicted phosphorylatable residue has been replaced by a non-phosphorylatable one. This protein although unable to bind ATP in vitro, is able to rescue the reversible ftsA2, the irreversible ftsA3 and, almost with the same efficiency, the ftsA16 amber alleles. Consequently, phosphorylation and ATP binding may not be essential for the function of FtsA. Alternatively they may have a regulatory role on the action of FtsA in the septator.

Titel:	Correlation between the structure and biochemical activities of FtsA, an essential cell division protein of the actin family.
Autor/in / Beteiligte Person:	Sánchez, M ; Valencia, A ; Ferrándiz, MJ ; Sander, C ; Vicente, M
Zeitschrift:	The EMBO journal, Jg. 13 (1994-10-17), Heft 20, S. 4919-25
Veröffentlichung:	2024- : [London] : Nature Publishing Group ; <i>Original Publication</i>: Eynsham, Oxford, England : Published for the European Molecular Biology Organization by IRL Press, [c1982-, 1994
Medientyp:	academicJournal
ISSN:	0261-4189 (print)
DOI:	10.1002/j.1460-2075.1994.tb06819.x
Schlagwort:	Actins chemistry Actins metabolism Adenosine Triphosphate metabolism Bacterial Proteins chemistry Bacterial Proteins metabolism Base Sequence Escherichia coli cytology Escherichia coli metabolism Models, Molecular Molecular Sequence Data Phosphorylation Protein Binding Protein Conformation Structure-Activity Relationship Actins physiology Bacterial Proteins physiology Cell Division physiology Escherichia coli Proteins
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article; Research Support, Non-U.S. Gov't Language: English [EMBO J] 1994 Oct 17; Vol. 13 (20), pp. 4919-25. MeSH Terms: Escherichia coli Proteins* ; Actins / physiology ; Bacterial Proteins / physiology ; Cell Division / *physiology ; Actins / chemistry ; Actins / metabolism ; Adenosine Triphosphate / metabolism ; Bacterial Proteins / chemistry ; Bacterial Proteins / metabolism ; Base Sequence ; Escherichia coli / cytology ; Escherichia coli / metabolism ; Models, Molecular ; Molecular Sequence Data ; Phosphorylation ; Protein Binding ; Protein Conformation ; Structure-Activity Relationship References: EMBO J. 1993 Oct;12(10):3957-65. (PMID: 8404863) ; J Biol Chem. 1972 Jun 25;247(12):3962-72. (PMID: 4555955) ; J Mol Biol. 1982 Jan 15;154(2):211-27. (PMID: 6804633) ; Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9513-7. (PMID: 1835085) ; J Bacteriol. 1984 Mar;157(3):779-84. (PMID: 6365891) ; Gene. 1986;48(1):119-31. (PMID: 3549457) ; Mol Microbiol. 1988 Sep;2(5):581-8. (PMID: 2846985) ; J Mol Biol. 1993 Mar 5;230(1):186-95. (PMID: 8450535) ; J Gen Microbiol. 1985 Feb;131(2):239-44. (PMID: 3884730) ; Cell. 1985 Oct;42(3):941-9. (PMID: 2996784) ; Nature. 1987 Aug 27-Sep 2;328(6133):766. (PMID: 3306399) ; Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7290-4. (PMID: 1323828) ; J Bacteriol. 1980 Feb;141(2):806-13. (PMID: 6988392) ; J Bacteriol. 1985 Nov;164(2):950-3. (PMID: 2414272) ; Nature. 1976 Nov 25;264(5584):328-33. (PMID: 794735) ; J Bacteriol. 1979 Nov;140(2):388-94. (PMID: 387733) ; Res Microbiol. 1991 Jul-Aug;142(6):623-31. (PMID: 1961975) ; J Mol Biol. 1973 Nov 15;80(4):575-99. (PMID: 4204102) ; J Bacteriol. 1987 Apr;169(4):1772-6. (PMID: 3031022) ; EMBO J. 1992 Jan;11(1):71-7. (PMID: 1740117) ; Cell. 1993 Jun 4;73(5):841-55. (PMID: 8500178) ; Trends Cell Biol. 1993 Feb;3(2):53-9. (PMID: 14731729) ; Nature. 1990 Sep 6;347(6288):37-44. (PMID: 2395459) ; J Bacteriol. 1986 Jun;166(3):985-92. (PMID: 3011758) ; J Bacteriol. 1992 Apr;174(7):2398-403. (PMID: 1551857) ; Science. 1990 Aug 3;249(4968):540-2. (PMID: 2200123) ; Nature. 1992 Sep 17;359(6392):251-4. (PMID: 1528267) ; Res Microbiol. 1991 Feb-Apr;142(2-3):253-7. (PMID: 1925025) ; Proc Natl Acad Sci U S A. 1993 Feb 1;90(3):1053-7. (PMID: 8430073) ; J Bacteriol. 1990 Sep;172(9):5097-102. (PMID: 2203741) ; J Biol Chem. 1975 May 25;250(10):4007-21. (PMID: 236308) ; Nature. 1990 Aug 16;346(6285):623-8. (PMID: 2143562) ; Nature. 1992 Sep 17;359(6392):254-6. (PMID: 1528268) ; Mol Microbiol. 1992 Sep;6(17):2517-24. (PMID: 1406287) ; Eur J Biochem. 1987 Nov 2;168(3):621-7. (PMID: 2822422) Substance Nomenclature: 0 (Actins) ; 0 (Bacterial Proteins) ; 0 (Escherichia coli Proteins) ; 0 (FtsA protein, Bacteria) ; 0 (FtsA protein, E coli) ; 8L70Q75FXE (Adenosine Triphosphate) Entry Date(s): Date Created: 19941017 Date Completed: 19941201 Latest Revision: 20220511 Update Code: 20240513 PubMed Central ID: PMC395432

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Correlation between the structure and biochemical activities of FtsA, an essential cell division protein of the actin family.