Abstract:
:To gain an understanding of structural changes induced in substrates by Escherichia coli ribonuclease P (RNase P), we have incorporated an interstrand disulfide crosslink proximal to the cleavage site in a model substrate. RNase P is able to process the reduced, non-crosslinked form of this substrate as well as a substrate in which the free thiol molecules have been alkylated with iodoacetamide. However, the oxidized, crosslinked form is cleaved at a significantly lower rate. Therefore, helical unwinding of the analog of the aminoacyl stem of the substrate near its site of cleavage may be necessary for efficient processing by E. coli RNase P.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Pomeranz Krummel DA,Kent O,MacMillan AM,Altman Sdoi
10.1006/jmbi.1999.3424keywords:
subject
Has Abstractpub_date
2000-02-04 00:00:00pages
1113-8issue
5eissn
0022-2836issn
1089-8638pii
S0022283699934241journal_volume
295pub_type
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更新日期:1997-05-23 00:00:00
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更新日期:2011-09-02 00:00:00
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pub_type: 杂志文章
doi:10.1006/jmbi.1995.0465
更新日期:1995-09-01 00:00:00