Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (90K) Freely available
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 (18)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Sears, L.
Right arrow Articles by Kong, H
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sears, L.
Right arrow Articles by Kong, H
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, Vol 24, Issue 18 3590-3592, Copyright © 1996 by Oxford University Press

ARTICLES

BaeI, another unusual BcgI-like restriction endonuclease

LE Sears, B Zhou, JM Aliotta, RD Morgan and H Kong
New England Biolabs, Inc., Beverly, MA 01915, USA.

BcgI and BcgI-like restriction endonucleases have a very distinct characteristic which causes them to differ from the other classified restriction enzymes; they all cleave double-stranded DNA specifically on both sides of the recognition sequence to excise a short DNA fragment including the recognition sites. Here we report a new BcgI- like restriction endonuclease, BaeI, isolated from Bacillus sphaericus. Like BcgI, BaeI also cleaves double-stranded DNA on both strands upstream and downstream of its recognition sequence (10/15)ACNNNNGTAYC(12/7). There are two dominant polypeptides in the final preparation of BaeI with molecular masses of approximately 80 and 55 kDa. Both are slightly larger than the two BcgI subunits. BaeI requires both Mg2+ and AdoMet to cleave DNA. Accompanying bilateral cleavage activity, the heteromeric BaeI also has an N6-adenine methyltransferase activity which modifies the symmetrically located adenines within its recognition sequence.
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
 MicrobiologyHome page
R. M. Dempsey, D. Carroll, H. Kong, L. Higgins, C. T. Keane, and D. C. Coleman
Sau42I, a BcgI-like restriction-modification system encoded by the Staphylococcus aureus quadruple-converting phage {pi}42
Microbiology, April 1, 2005; 151(4): 1301 - 1311.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
P. M. Skowron, J. Majewski, A. Zylicz-Stachula, S. M. Rutkowska, I. Jaworowska, and R. I. Harasimowicz-Slowinska
A new Thermus sp. class-IIS enzyme sub-family: isolation of a 'twin' endonuclease TspDTI with a novel specificity 5'-ATGAA(N11/9)-3', related to TspGWI, TaqII and Tth111II
Nucleic Acids Res., July 15, 2003; 31(14): e74 - e74.
[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.