ASIA unversity:Item 310904400/8015
English  |  正體中文  |  简体中文  |  Items with full text/Total items : 90120/105278 (86%)
Visitors : 8950277      Online Users : 65
RC Version 6.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
Scope Tips:
  • please add "double quotation mark" for query phrases to get precise results
  • please goto advance search for comprehansive author search
  • Adv. Search
    HomeLoginUploadHelpAboutAdminister Goto mobile version

    Please use this identifier to cite or link to this item:

    Title: Role of the substrate conformation and of the S1 protein in the cleavage efficiency of the T4 endoribonuclease RegB.
    Authors: Lebars I;Hu RM, Lallem;JY, Uzan M;Bontems F.
    Contributors: Department of Biotechnology
    Date: 2001
    Issue Date: 2010-03-15 16:11:28 (UTC+8)
    Publisher: Asia University
    Abstract: The T4 endoribonuclease RegB is involved in the inactivation of the phage early messengers. It cuts specifically in the middle of GGAG sequences found in early messenger intergenic regions but not GGAG sequences located in coding sequences or in late messengers. In vitro RegB activity is very low but is enhanced by a factor up to 100 by the ribosomal protein S1. In the absence of clear sequence motif distinguishing substrate and non-substrate GGAG-containing RNAs, we
    postulated the existence of a structural determinant. To test this hypothesis, we correlated the structure, probed by NMR spectroscopy, with the cleavage propensity of short RNA molecules derived from an artificial substrate. A kinetic analysis of the cleavage was performed in the presence and absence of S1. In the absence of S1, RegB efficiently hydrolyses substrates in which the last G of the GGAG motif is located in a short stem between two loops. Both strengthening and weakening of this structure strongly decrease the cleavage rate, indicating that this structure constitutes a positive cleavage
    determinant. Based on our results and those of others, we speculate that S1 favors the formation of the structure recognized by RegB and can thus be considered a “presentation protein.”
    Relation: The Journal of Biological Chemistry 276(16):13264-72
    Appears in Collections:[Department of Biotechnology] Journal Article

    Files in This Item:

    File Description SizeFormat
    310904400-8015.doc35KbMicrosoft Word140View/Open

    All items in ASIAIR are protected by copyright, with all rights reserved.

    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback