Skip Navigation

This Article
Right arrow Print PDF (1531K)
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 Tomaschewski, J.
Right arrow Articles by Rüger, W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tomaschewski, J.
Right arrow Articles by Rüger, W.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1985, Vol. 13, No. 21 7551-7566
© 1985

Articles

T4-induced {alpha}- and ß-glucosyltransferase: cloning of the genes and a comparison of their products based on sequencing data

Jörg Tomaschewski, Hermann Gram, John W. Crabb1,* and Wolfgang Rüger+

Arbeitsgruppe Molekulare Genetik, Lehrstuhl Biologie der Mikroorgarismen 1Protein Sequenzierungslaboratorium, Institut für Physiologische Chemie I, Ruhr-Universität Bochum D-4630 Bochum 1, FRG

+To whom correspondence should be addressed

Received September 23, 1985. Accepted October 11, 1985.

Bacteriophage T4 {alpha}- and ß-glucosyltransferases link glucosyl units to the 5-HMdC residues of its DNA. The monoglucosyl group in {alpha}-linkage predominates over the one in ß linkage. Having recently reported on the nucleotide sequence of gene {alpha}gt (1) we now determined the nucleotide sequence of gene ßgt. The genes were each cloned on a high expression vector under the control of the {lambda}pL promoter. After thermo-induction the proteins were isolated and purified to homogeneity. To verify that the translational starting sites and the proposed reading frames are effective in vivo the sequence of the first 31 amino acid residues from gp{alpha}gt and the first 30 amino acid residues from gpßgt were determined by Edman degradation.

The primary structures of the two proteins seem to have only limited structural similarities. The results are discussed comparing secondary structure predictions and homologies with other proteins from the protein sequence database of the Protein Identification Resource.

*Present address: W.Alton Jones Cell Science Center Lake Placid, New York, N.Y. 12946, USA


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
 Microbiol. Mol. Biol. Rev.Home page
E. S. Miller, E. Kutter, G. Mosig, F. Arisaka, T. Kunisawa, and W. Ruger
Bacteriophage T4 Genome
Microbiol. Mol. Biol. Rev., March 1, 2003; 67(1): 86 - 156.
[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.