Skip Navigation

This Article
Right arrow Print PDF (1224K)
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 (107)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Som, S.
Right arrow Articles by Friedman, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Som, S.
Right arrow Articles by Friedman, S.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1987, Vol. 15, No. 1 313-332
© 1987

Articles

Nucleotide sequence and expression of the gene encoding the EcoRII modification enzyme

Subhendu Som, Ashok S. Bhagwat+ and Stanley Friedman

+Cold Spring Harbor Laboratory, PO Box 100, Cold Spring Harbor NY 11724, USA Department of Pharmacology, SUNY-Health Science Center, 450 Clarkson Avenue Brooklyn, NY 11203

Received August 20, 1986. Revised October 27, 1986. Accepted November 17, 1986.

The gene coding for the EcoRII modification enzyme has been cloned and the nucleotide sequence of 1933 base pairs containing the gene has been determined. The gene codes for a protein of 477 amino acids. Two transcriptional start sites have been mapped by S1 mapping. One deletion that removes 34 N-terminal amino acids was found to have partial enzyme activity. Comparison of the EcoRII methylase sequence with other cytosine methylases revealed several domains of partial homology among all cytosine methylases. Cloning the gene in multicopy pUC vectors increased the expression by 6–18 fold. A 40 fold overproduction of the EcoRII methylase was obtained by cloning the gene in the expression vector carrying the lambda PL promoter.


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. Bacteriol.Home page
S. Ohno, N. Handa, M. Watanabe-Matsui, N. Takahashi, and I. Kobayashi
Maintenance Forced by a Restriction-Modification System Can Be Modulated by a Region in Its Modification Enzyme Not Essential for Methyltransferase Activity
J. Bacteriol., March 15, 2008; 190(6): 2039 - 2049.
[Abstract] [Full Text] [PDF]

Home page
 Antimicrob. Agents Chemother.Home page
Y.-T. Chen, H.-Y. Shu, L.-H. Li, T.-L. Liao, K.-M. Wu, Y.-R. Shiau, J.-J. Yan, I.-J. Su, S.-F. Tsai, and T.-L. Lauderdale
Complete Nucleotide Sequence of pK245, a 98-Kilobase Plasmid Conferring Quinolone Resistance and Extended-Spectrum-{beta}-Lactamase Activity in a Clinical Klebsiella pneumoniae Isolate
Antimicrob. Agents Chemother., November 1, 2006; 50(11): 3861 - 3866.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
C. K. Sherburne, T. D. Lawley, M. W. Gilmour, F. R. Blattner, V. Burland, E. Grotbeck, D. J. Rose, and D. E. Taylor
The complete DNA sequence and analysis of R27, a large IncHI plasmid from Salmonella typhi that is temperature sensitive for transfer
Nucleic Acids Res., May 15, 2000; 28(10): 2177 - 2186.
[Abstract] [Full Text] [PDF]

Home page
 Appl. Environ. Microbiol.Home page
R. Morgan, J.-p. Xiao, and S.-y. Xu
Characterization of an Extremely Thermostable Restriction Enzyme, PspGI, from a Pyrococcus Strain and Cloning of the PspGI Restriction-Modification System in Escherichia coli
Appl. Envir. Microbiol., October 1, 1998; 64(10): 3669 - 3673.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
J. C. Pepe and S. Lory
Amino Acid Substitutions in PilD, a Bifunctional Enzyme of Pseudomonas aeruginosa. EFFECT ON LEADER PEPTIDASE AND N-METHYLTRANSFERASE ACTIVITIES IN VITRO AND IN VIVO
J. Biol. Chem., July 24, 1998; 273(30): 19120 - 19129.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B. Bandaru, J. Gopal, and A. S. Bhagwat
Overproduction of DNA Cytosine Methyltransferases Causes Methylation and C [IMAGE] T Mutations at Non-canonical Sites
J. Biol. Chem., March 29, 1996; 271(13): 7851 - 7859.
[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.