NDLI: Electrospray mass spectrometric investigation of the chaperone SecB.

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Electrospray mass spectrometric investigation of the chaperone SecB.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Smith, V. F. Schwartz, B. L. Smith, R. D. Randall, L. L.
Description	Country affiliation: United States Author Affiliation: Smith VF ( Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660, USA.)
Abstract	Electrospray ionization mass spectrometry was used to investigate the structure of the Escherichia coli chaperone protein SecB. It was determined that the N-terminal methionine of SecB has been removed and that more than half of all SecB monomers are additionally modified, most likely by acetylation of the N-terminus or a lysine. The use of gentle mass spectrometer interface conditions showed that the predominant, oligomeric form of SecB is a tetramer that is stable over a range of solution pH conditions and mass spectrometer interface heating (i.e., inlet capillary temperatures). At very high pH, SecB dimers are observed. SecB contains a region that is hypersensitive to cleavage by proteinase K and is thought to be involved in conformational changes that are crucial to the function of SecB. We identified the primary site of cleavage to be between Leu 141 and Gln 142. Fourteen amino acids are removed, but the truncated form remains a tetramer with stability similar to that of the intact form.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	3
Volume Number	5
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1996-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proteins Chemistry Escherichia Coli Metabolism Molecular Chaperones Chromatography, Gel Endopeptidase K Pharmacology Hydrogen-ion Concentration Mass Spectrometry Molecular Weight Protein Conformation Temperature Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s. Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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