| Escherichia coli Single-Stranded DNA-Binding Protein: NanoESI-MS Studies of Salt-Modulated Subunit Exchange and DNA Binding Transactions. | |
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MedLine Citation:
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PMID: 23283730 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Single-stranded DNA-binding proteins (SSBs) are ubiquitous oligomeric proteins that bind with very high affinity to single-stranded DNA and have a variety of essential roles in DNA metabolism. Nanoelectrospray ionization mass spectrometry (nanoESI-MS) was used to monitor subunit exchange in full-length and truncated forms of the homotetrameric SSB from Escherichia coli. Subunit exchange in the native protein was found to occur slowly over a period of hours, but was significantly more rapid in a truncated variant of SSB from which the eight C-terminal residues were deleted. This effect is proposed to result from C-terminus mediated stabilization of the SSB tetramer, in which the C-termini interact with the DNA-binding cores of adjacent subunits. NanoESI-MS was also used to examine DNA binding to the SSB tetramer. Binding of single-stranded oligonucleotides [one molecule of (dT)(70), one molecule of (dT)(35), or two molecules of (dT)(35)] was found to prevent SSB subunit exchange. Transfer of SSB tetramers between discrete oligonucleotides was also observed and is consistent with predictions from solution-phase studies, suggesting that SSB-DNA complexes can be reliably analyzed by ESI mass spectrometry. |
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Authors:
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Claire E Mason; Slobodan Jergic; Allen T Y Lo; Yao Wang; Nicholas E Dixon; Jennifer L Beck |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2013-1-3 |
Journal Detail:
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Title: Journal of the American Society for Mass Spectrometry Volume: - ISSN: 1879-1123 ISO Abbreviation: J. Am. Soc. Mass Spectrom. Publication Date: 2013 Jan |
Date Detail:
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Created Date: 2013-1-3 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9010412 Medline TA: J Am Soc Mass Spectrom Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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School of Chemistry, University of Wollongong, Wollongong, NSW, Australia. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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