FASEB J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Huber, P. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Huber, P. W.

The FASEB Journal, Vol 7, 1367-1375, Copyright © 1993 by The Federation of American Societies for Experimental Biology


REVIEWS

Chemical nucleases: their use in studying RNA structure and RNA-protein interactions

PW Huber
Department of Chemistry and Biochemistry, University of Notre Dame, Indiana 46556.

Metal complexes that cleave nucleic acids provide a new means to study RNA structure and RNA-protein interactions. Methods that use these chemical nucleases help compensate for the limitations of other techniques used to determine structure. Because the ligands that coordinate the metal generally control the cleavage selectivity of these complexes, it has become possible to design nucleolytic reagents that target specific higher-order structures. In combination with site- directed mutagenesis these conformation-specific probes can be used to delineate long-range interactions. Alternatively, complexes that cut irrespective of sequence and secondary structure have been used in protection (foot-printing) experiments to locate protein binding sites. Because each position of the nucleic acid is susceptible to cleavage, the protection pattern yields a highly resolved definition of the contact site between the protein and RNA. In other applications, metal complexes have been conjugated to functional moieties such as oligonucleotides, peptides, or substrate analogs to direct their binding to a distinct site on a specific RNA molecule. This latter strategy holds significant therapeutic promise for the destruction of pathogenic RNAs.


This article has been cited by other articles:


Home page
RNAHome page
S. Niranjanakumari, J. J. Day-Storms, M. Ahmed, J. Hsieh, N. H. Zahler, R. A. Venters, and C. A. Fierke
Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavage
RNA, April 1, 2007; 13(4): 521 - 535.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
N. G. Beloglazova, M. M. Fabani, M. A. Zenkova, E. V. Bichenkova, N. N. Polushin, V. V. Sil'nikov, K. T. Douglas, and V. V. Vlassov
Sequence-specific artificial ribonucleases. I. Bis-imidazole-containing oligonucleotide conjugates prepared using precursor-based strategy
Nucleic Acids Res., July 23, 2004; 32(13): 3887 - 3897.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. L. Rawlings, G. D. Matt, and P. W. Huber
Analysis of the Binding of Xenopus Transcription Factor IIIA to Oocyte 5 S rRNA and to the 5 S rRNA Gene
J. Biol. Chem., January 12, 1996; 271(2): 869 - 877.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1993 by The Federation of American Societies for Experimental Biology.