Advertisement
JBC

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


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Thorogood, H.
Right arrow Articles by Connolly, B. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Thorogood, H.
Right arrow Articles by Connolly, B. A.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Volume 271, Number 15, Issue of April 12, 1996 pp. 8855-8862
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
Influence of the Phosphate Backbone on the Recognition and Hydrolysis of DNA by the EcoRV Restriction Endonuclease
A STUDY USING OLIGODEOXYNUCLEOTIDE PHOSPHOROTHIOATES

(Received for publication, November 3, 1995; and in revised form, January 31, 1996)

Harry Thorogood Jane A. Grasby Bernard A. Connolly

A set of phosphorothioate-containing oligonucleotides based on pGACGATATCGTC, a self-complementary dodecamer that contains the EcoRV recognition sequence (GATATC), has been prepared. The phosphorothioate group has been individually introduced at the central nine phosphate positions and the two diastereomers produced at each site separated and purified. The K and V(max) values found for each of these modified DNA molecules with the EcoRV restriction endonuclease have been determined and compared with those seen for the unmodified all-phosphate-containing dodecamer. This has enabled an evaluation of the roles that both of the non-esterified oxygen atoms in the individual phosphates play in DNA binding and hydrolysis by the endonuclease. The results have also been compared with crystal structures of the EcoRV endonuclease, complexed with an oligodeoxynucleotide, to allow further definition of phosphate group function during substrate binding and turnover. For further study, see the related article ``Probing the Indirect Readout of the Restriction Enzyme EcoRV: Mutational Analysis of Contacts to the DNA Backbone'' (Wenz, A., Jeltsch, A., and Pingoud, A. (1996) J. Biol. Chem. 271, 5565-5573).




Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Nucleic Acids ResHome page
S. An, G. Barany, and K. Musier-Forsyth
Evolution of acceptor stem tRNA recognition by class II prolyl-tRNA synthetase
Nucleic Acids Res., May 1, 2008; 36(8): 2514 - 2521.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
E. Armalyte, J. M. Bujnicki, J. Giedriene, G. Gasiunas, J. Kosinski, and A. Lubys
Mva1269I: A Monomeric Type IIS Restriction Endonuclease from Micrococcus Varians with Two EcoRI- and FokI-like Catalytic Domains
J. Biol. Chem., December 16, 2005; 280(50): 41584 - 41594.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
A. Pingoud and A. Jeltsch
Structure and function of type II restriction endonucleases
Nucleic Acids Res., September 15, 2001; 29(18): 3705 - 3727.
[Abstract] [Full Text] [PDF]


Home page
Protein Eng Des SelHome page
T. Lanio, A. Jeltsch, and A. Pingoud
On the possibilities and limitations of rational protein design to expand the specificity of restriction enzymes: a case study employing EcoRV as the target
Protein Eng. Des. Sel., April 1, 2000; 13(4): 275 - 281.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
N. C. Horton, K. J. Newberry, and J. J. Perona
Metal ion-mediated substrate-assisted catalysis in type II restriction endonucleases
PNAS, November 10, 1998; 95(23): 13489 - 13494.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
N. C. Horton and J. J. Perona
Recognition of Flanking DNA Sequences by EcoRV Endonuclease Involves Alternative Patterns of Water-mediated Contacts
J. Biol. Chem., August 21, 1998; 273(34): 21721 - 21729.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
H. E. Johansson, D. Dertinger, K. A. LeCuyer, L. S. Behlen, C. H. Greef, and O. C. Uhlenbeck
A thermodynamic analysis of the sequence-specific binding of RNA by bacteriophage MS2 coat protein
PNAS, August 4, 1998; 95(16): 9244 - 9249.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement