Skip Navigation

This Article
Right arrow Print PDF (3915K)
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 arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Hsi, K.-L.
Right arrow Articles by Wang, T. S.-F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hsi, K.-L.
Right arrow Articles by Wang, T. S.-F.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1990, Vol. 18, No. 21 6231-6237
© 1990

ENZYMOLOGY

Human DNA polymerase {alpha} catalytic polypeptide binds ConA and RCA and contains a specific labile site in the N-terminus

Kuo-Liang Hsi, William C. Copeland and Teresa S.-F. Wang*

Laboratory of Experimental Oncology, Department of Pathology, Stanford University School of Medicine Stanford, CA 94305, USA

*To whom correspondence should be addressed

Received August 9, 1990. Revised October 2, 1990. Accepted October 2, 1990.

The catalytic polypeptide of DNA polymerase {alpha} is often observed in vitro as a family of phosphopolypeptides predominantly of 180 and 165 kDa derived from a single primary structure. The estimated Mr of this polypeptide deduced from the full-length cDNA is 165 kDa. Immunoblot analysis with polyclonal antibodies against peptldes of the N- and C-terminl of the deduced primary sequence indicates that the observed family of polypetldes from 180 kDa to lower molecular weight results from proteolytic cleavage from the N-termlnus. Antibodies against the N-terminal peptide detect only the 180 kDa species suggesting that this higher molecular weight polypeptide may be the result of posttranslational modification of the 165 kDa primary translation product. The catalytic polypeptide is not only phosphorylated but is also found to react with lectins ConA and RCA. N-terminal sequencing of the isolated catalytic polypeptide from human cells and of the recombinant fusion proteins indicates that the often observed 165 kDa polypeptide is the in vitro proteolytic cleavage product of the modified 180 kDa protein at the specific site between lys123 and lys124 within the sequence -RNVKKLAVTKPNN-.


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
 J HeredHome page
A. K. Shasany, M. P. Darokar, S. Dhawan, A. K. Gupta, S. Gupta, A. K. Shukla, N. K. Patra, and S. P. S. Khanuja
Use of RAPD and AFLP Markers to Identify Inter- and Intraspecific Hybrids of Mentha
J. Hered., September 1, 2005; 96(5): 542 - 549.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
T. Mizuno, N. Ito, M. Yokoi, A. Kobayashi, K. Tamai, H. Miyazawa, and F. Hanaoka
The Second-Largest Subunit of the Mouse DNA Polymerase alpha -Primase Complex Facilitates Both Production and Nuclear Translocation of the Catalytic Subunit of DNA Polymerase alpha
Mol. Cell. Biol., June 1, 1998; 18(6): 3552 - 3562.
[Abstract] [Full Text]

Home page
 Proc. Natl. Acad. Sci. USAHome page
D. S. Levin, W. Bai, N. Yao, M. O'Donnell, and A. E. Tomkinson
An interaction between DNA ligase I and proliferating cell nuclear antigen: Implications for Okazaki fragment synthesis and joining
PNAS, November 25, 1997; 94(24): 12863 - 12868.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
O. Schub, G. Rohaly, R. W. P. Smith, A. Schneider, S. Dehde, I. Dornreiter, and H.-P. Nasheuer
Multiple Phosphorylation Sites of DNA Polymerase alpha -Primase Cooperate to Regulate the Initiation of DNA Replication in Vitro
J. Biol. Chem., October 5, 2001; 276(41): 38076 - 38083.
[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.