Skip Navigation

This Article
Right arrow Print PDF (2657K)
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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (39)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Kleinschmidt, A. M.
Right arrow Articles by Martinson, H. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kleinschmidt, A. M.
Right arrow Articles by Martinson, H. G.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1981, Vol. 9, No. 11 2423-2431
© 1981

MOLECULAR BIOLOGY

Structure of nucleosome core particles containing uH2A (A24)

Ann M. Kleinschmidt and Harold G. Martinson

Division of Biochemistry, Department of Chemistry, and The Molecular Biology Institute, University of California Los Angeles, CA 90024, USA

Received April 20, 1981. We have purified uH2A (A24) and reconstituted it, in place of H2A, into high molecular weight nucleohistone containing the core histones and DNA. uH2A-containing core particles were then prepared by nuclease digestion and studies on these particles were carried out. We show that two uH2A molecules can be accommodated within a core particle. We also show that the presence of two uH2A molecules in a core particle does not alter significantly either the pattern or the rate of DNase I digestion as compared to both reconstituted and native core particles. Finally, we show that HMG proteins 14 and 17 can bind to uH2A-containing core particles. We conclude that uH2A has little influence on structure at the level of individual nucleosomes.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Proc. Natl. Acad. Sci. USAHome page
M. G. Kapetanaki, J. Guerrero-Santoro, D. C. Bisi, C. L. Hsieh, V. Rapic-Otrin, and A. S. Levine
The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites
PNAS, February 21, 2006; 103(8): 2588 - 2593.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. J. M. Jason, R. M. Finn, G. Lindsey, and J. Ausio
Histone H2A Ubiquitination Does Not Preclude Histone H1 Binding, but It Facilitates Its Association with the Nucleosome
J. Biol. Chem., February 11, 2005; 280(6): 4975 - 4982.
[Abstract] [Full Text] [PDF]

Home page
 Genes Dev.Home page
Y. Zhang
Transcriptional regulation by histone ubiquitination and deubiquitination
Genes & Dev., November 15, 2003; 17(22): 2733 - 2740.
[Full Text] [PDF]

Home page
 J. Cell Biol.Home page
B. P. Chadwick and H. F. Willard
A Novel Chromatin Protein, Distantly Related to Histone H2A, Is Largely Excluded from the Inactive X Chromosome
J. Cell Biol., January 22, 2001; 152(2): 375 - 384.
[Abstract] [Full Text] [PDF]

Home page
 Genes Dev.Home page
P Sung, S Prakash, and L Prakash
The RAD6 protein of Saccharomyces cerevisiae polyubiquitinates histones, and its acidic domain mediates this activity.
Genes & Dev., November 1, 1988; 2(11): 1476 - 1485.
[Abstract] [PDF]

Home page
 J. Biol. Chem.Home page
L. J. M. Jason, S. C. Moore, J. Ausio, and G. Lindsey
Magnesium-dependent Association and Folding of Oligonucleosomes Reconstituted with Ubiquitinated H2A
J. Biol. Chem., April 27, 2001; 276(18): 14597 - 14601.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.