Advertisement
JBC

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


     

Originally published In Press as doi:10.1074/jbc.M109000200 on November 7, 2001

J. Biol. Chem., Vol. 277, Issue 2, 958-966, January 11, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
277/2/958    most recent
M109000200v1
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 Sabatini, R.
Right arrow Articles by Borst, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sabatini, R.
Right arrow Articles by Borst, P.
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?

Recognition of Base J in Duplex DNA by J-binding Protein*

Robert SabatiniDagger §, Nico Meeuwenoord||, Jacques H. van Boom||, and Piet BorstDagger

From the Dagger  Division of Molecular Biology and Centre for Biomedical Genetics, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands, the || Leiden Institute of Chemistry, Gorlaeus Laboratories, 2300 RA Leiden, The Netherlands, and the § Division of Geographic Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294

beta -D-Glucosylhydroxymethyluracil, also called base J, is an unusual modified DNA base conserved among Kinetoplastida. Base J is found predominantly in repetitive DNA and correlates with epigenetic silencing of telomeric variant surface glycoprotein genes. We have previously found a J-binding protein (JBP) in Trypanosoma, Leishmania, and Crithidia. We have now characterized the binding properties of recombinant JBP from Crithidia using synthetic J-DNA substrates that contain the glycosylated base in various DNA sequences. We find that JBP recognizes base J only when presented in double-stranded DNA but not in single-stranded DNA or in an RNA:DNA duplex. It also fails to interact with free glucose or free base J. JBP is unable to recognize nonmodified DNA or intermediates of J synthesis, suggesting that JBP is not directly involved in J biosynthesis. JBP binds J-DNA with high affinity (Kd = 40-140 nM) but requires at least 5 bp flanking the glycosylated base for optimal binding. The nature of the flanking sequence affects binding because J in a telomeric sequence binds JBP with higher affinity than J in another sequence known to contain J in trypanosome DNA. We conclude that JBP is a structure-specific DNA-binding protein. The significance of these results in relation to the biological role and mechanism of action of J modification in kinetoplastids is discussed.

* This work was supported in part by The Netherlands Foundation for Chemical Research and The Netherlands Organization for Scientific Research (to P. B.).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.

To whom correspondence should be addressed. Tel.: 205-934-1971; Fax: 205-975-2547; E-mail: sabatini@uab.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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
L. J. Cliffe, R. Kieft, T. Southern, S. R. Birkeland, M. Marshall, K. Sweeney, and R. Sabatini
JBP1 and JBP2 are two distinct thymidine hydroxylases involved in J biosynthesis in genomic DNA of African trypanosomes
Nucleic Acids Res., April 1, 2009; 37(5): 1452 - 1462.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
Z. Yu, P.-A. Genest, B. ter Riet, K. Sweeney, C. DiPaolo, R. Kieft, E. Christodoulou, A. Perrakis, J. M. Simmons, R. P. Hausinger, et al.
The protein that binds to DNA base J in trypanosomatids has features of a thymidine hydroxylase
Nucleic Acids Res., April 1, 2007; 35(7): 2107 - 2115.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
B. Li, A. Espinal, and G. A. M. Cross
Trypanosome Telomeres Are Protected by a Homologue of Mammalian TRF2
Mol. Cell. Biol., June 15, 2005; 25(12): 5011 - 5021.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
P.-A. Genest, B. t. Riet, C. Dumas, B. Papadopoulou, H. G. A. M. van Luenen, and P. Borst
Formation of linear inverted repeat amplicons following targeting of an essential gene in Leishmania
Nucleic Acids Res., March 21, 2005; 33(5): 1699 - 1709.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. Sabatini, N. Meeuwenoord, J. H. van Boom, and P. Borst
Site-specific Interactions of JBP with Base and Sugar Moieties in Duplex J-DNA. EVIDENCE FOR BOTH MAJOR AND MINOR GROOVE CONTACTS
J. Biol. Chem., July 26, 2002; 277(31): 28150 - 28156.
[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.
Advertisement
spacer
Advertisement
Advertisement