DOI: 10.1110/ps.4090102. Complex behavior in solution of homodimeric SecA

Complex behavior in solution of homodimeric SecA

10.1110/ps.4090102

Crossref journal-article

Wiley

Protein Science (311)

Abstract

AbstractSecA, a homodimeric protein involved in protein export in Escherichia coli, exists in the cell both associated with the membrane translocation apparatus and free in the cytosol. SecA is a multifunctional protein involved in protein localization and regulation of its own expression. To carry out these functions, SecA interacts with a variety of proteins, phospholipids, nucleotides, and nucleic acid and shows two enzymic activities. It is an ATPase and a helicase. Its role during protein localization involves interaction with the precursor polypeptides to be exported, the cytosolic chaperone SecB, and the SecY subunit of the membrane‐associated translocase, as well as with acidic phospholipids. At the membrane, SecA undergoes a cycle of binding and hydrolysis of ATP coupled to conformational changes that result in translocation of precursors through the cytoplasmic membrane. The helicase activity of SecA and its affinity for its mRNA are involved in regulation of its own expression. SecA has been reported to exist in at least two conformational states during its functional cycle. Here we have used analytical centrifugation, as well as column chromatography coupled with multiangle light scatter, to show that in solution SecA undergoes at least two monomer‐dimer equilibrium reactions that are sensitive to temperature and to concentration of salt.

Bibliography

Woodbury, R. L., Hardy, S. J. S., & Randall, L. L. (2002). Complex behavior in solution of homodimeric SecA. Protein Science, 11(4), 875â882. Portico.

Authors 3

Ronald L. Woodbury (first)
Simon J.S. Hardy (additional)
Linda L. Randall (additional)

References 22 Referenced 115

10.1016/0006-291X(91)90507-4
10.1016/S0021-9258(18)54245-9
10.1016/S0021-9258(19)57471-3
10.1016/0022-2836(91)90212-O
10.1128/JB.180.3.527-537.1998 / J. Bacteriol. / Identification and characterization of protease‐resistant SecA fragments: secA has two membrane‐integral forms by Chen X. (1998)
10.1016/S0006-3495(97)78680-6
10.1021/bi000299y
10.1021/bi00211a030
10.1021/bi982818r
10.1128/MMBR.63.1.161-173.1999
10.1016/0014-5793(89)80516-2
10.1016/S0021-9258(18)43969-5 / J. Biol. Chem. / Deducing the organization of a transmembrane domain by disulfide cross‐linking. The bacterial chemoreceptor Trg by Lee G.F. (1994)
{'key': 'e_1_2_7_14_1', 'first-page': '614', 'article-title': 'On the role of intramolecular potassium in protein synthesis', 'volume': '80', 'author': 'Lubin M.', 'year': '1964', 'journal-title': 'Biochim. Biophys. Acta.'} / Biochim. Biophys. Acta. / On the role of intramolecular potassium in protein synthesis by Lubin M. (1964)
10.1074/jbc.274.13.8993
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10.1074/jbc.M002885200
10.1021/bi992062b

Dates

Type	When
Created	23 years, 1 month ago (July 26, 2002, 7:59 p.m.)
Deposited	1 year, 10 months ago (Oct. 8, 2023, 8:22 a.m.)
Indexed	4 weeks ago (July 30, 2025, 8:22 p.m.)
Issued	23 years, 4 months ago (April 1, 2002)
Published	23 years, 4 months ago (April 1, 2002)
Published Online	16 years, 7 months ago (Jan. 1, 2009)
Published Print	23 years, 4 months ago (April 1, 2002)

Funders 0

None

BibTeX

@article{Woodbury_2002, title={Complex behavior in solution of homodimeric SecA}, volume={11}, ISSN={1469-896X}, url={http://dx.doi.org/10.1110/ps.4090102}, DOI={10.1110/ps.4090102}, number={4}, journal={Protein Science}, publisher={Wiley}, author={Woodbury, Ronald L. and Hardy, Simon J.S. and Randall, Linda L.}, year={2002}, month=apr, pages={875–882} }

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