JBC INTERFERin siRNA transfection reagent

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


     


Originally published In Press as doi:10.1074/jbc.M110342200 on December 27, 2001

J. Biol. Chem., Vol. 277, Issue 10, 7703-7712, March 8, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
277/10/7703    most recent
M110342200v1
Right arrow Alert me when this article is cited
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Goldhaber-Gordon, I.
Right arrow Articles by Baker, T. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Goldhaber-Gordon, I.
Right arrow Articles by Baker, T. A.

Sequence and Positional Requirements for DNA Sites in a Mu Transpososome*

Ilana Goldhaber-GordonDagger , Michael H. EarlyDagger , Matthew K. Gray, and Tania A. BakerDagger §||

From the Dagger  Department of Biology and § Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 and  Newbury Networks, Inc., Boston, Massachusetts 02116

Transposition of bacteriophage Mu uses two DNA cleavage sites and six transposase recognition sites, with each recognition site divided into two half-sites. The recognition sites can activate transposition of non-Mu DNA sequences if a complete set of Mu sequences is not available. We have analyzed 18 sequences from a non-Mu DNA molecule, selected in a functional assay for the ability to be transposed by MuA transposase. These sequences are remarkably diverse. Nonetheless, when viewed as a group they resemble a Mu DNA end, with a cleavage site and a single recognition site. Analysis of these "pseudo-Mu ends" indicates that most positions in the cleavage and recognition sites contribute sequence-specific information that helps drive transposition, though only the strongest contributors are apparent from mutagenesis data. The sequence analysis also suggests variability in the alignment of recognition half-sites. Transposition assays of specifically designed DNA substrates support the conclusion that the transposition machinery is flexible enough to permit variability in half-site spacing and also perhaps variability in the placement of the recognition site with respect to the cleavage site. This variability causes only local perturbations in the protein-DNA complex, as indicated by experiments in which altered and unaltered DNA substrates are paired.


* This work was supported by United States Public Health Service Grant GM499224 from the National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| Employee of the Howard Hughes Medical Institute. To whom correspondence should be addressed: Howard Hughes Medical Inst., Massachusetts Inst. of Technology, 77 Massachusetts Ave., 68-523 Cambridge, MA 02139. E-mail: tabaker@mit.edu.


Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


This article has been cited by other articles:


Home page
Nucleic Acids ResHome page
A.-H. Saariaho and H. Savilahti
Characteristics of MuA transposase-catalyzed processing of model transposon end DNA hairpin substrates
Nucleic Acids Res., June 6, 2006; 34(10): 3139 - 3149.
[Abstract] [Full Text] [PDF]


Home page
Genes Dev.Home page
J. F. Yuan, D. R. Beniac, G. Chaconas, and F. P. Ottensmeyer
3D reconstruction of the Mu transposase and the Type 1 transpososome: a structural framework for Mu DNA transposition
Genes & Dev., April 1, 2005; 19(7): 840 - 852.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
I. Goldhaber-Gordon, T. L. Williams, and T. A. Baker
DNA Recognition Sites Activate MuA Transposase to Perform Transposition of Non-Mu DNA
J. Biol. Chem., March 1, 2002; 277(10): 7694 - 7702.
[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 © 2002 by the American Society for Biochemistry and Molecular Biology.