Skip Navigation

This Article
Right arrow Print PDF (775K)
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 (44)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Watanabe, K.
Right arrow Articles by Kimura, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Watanabe, K.
Right arrow Articles by Kimura, A.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1986, Vol. 14, No. 11 4393-4400
© 1986

Articles

The nudeotide sequence of the gene for {gamma}-glutamylcysteine synthetase of Escherichia coli

Kunihiko Watanabe*, Yoshinori Yamano, Kousaku Murata and Akira Kimura

Research Institute for Food Science, Kyoto University Uji, Kyoto 611, Japan

*To whom correspondence should be addressed

Received May 1, 1986. Accepted May 15, 1986.

The nudeotide sequence of the gsh I gene for {gamma}- glutamylcysteine synthetase(GSH I) of Escherichia coli B has been determined. The gsh I structural gene contains 1557 bases in length and predicted a ploypeptide of 518 amino acids with a calculated molecular weight of 58,251. The value is in good agreement with that obtained from gel filtration and SDS/PAGE of GSH I. The initiation codon 5 bp downstream of putative Shine- Dalgarno sequence was an unusual TTG, which encoded methionine. For transcription, two sets of consensus promoter signals(–10 and –35 regions) overlapping each other were identified. The terminator signal shows the favored stem-loop structure with an adequate free energy {bigtriangleup}G = –22.80 kcal/mol.


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
L. Malki, M. Yanku, I. Borovok, G. Cohen, M. Mevarech, and Y. Aharonowitz
Identification and Characterization of gshA, a Gene Encoding the Glutamate-Cysteine Ligase in the Halophilic Archaeon Haloferax volcanii
J. Bacteriol., August 15, 2009; 191(16): 5196 - 5204.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. J. Abbott, J. Pei, J. L. Ford, Y. Qi, V. N. Grishin, L. A. Pitcher, M. A. Phillips, and N. V. Grishin
Structure Prediction and Active Site Analysis of the Metal Binding Determinants in gamma -Glutamylcysteine Synthetase
J. Biol. Chem., November 2, 2001; 276(45): 42099 - 42107.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
G. Creissen, J. Firmin, M. Fryer, B. Kular, N. Leyland, H. Reynolds, G. Pastori, F. Wellburn, N. Baker, A. Wellburn, et al.
Elevated Glutathione Biosynthetic Capacity in the Chloroplasts of Transgenic Tobacco Plants Paradoxically Causes Increased Oxidative Stress
PLANT CELL, July 1, 1999; 11(7): 1277 - 1292.
[Abstract] [Full Text]

Home page
 Plant Physiol.Home page
G. Noctor, A.-C. M. Arisi, L. Jouanin, and C. H. Foyer
Manipulation of Glutathione and Amino Acid Biosynthesis in the Chloroplast
Plant Physiology, October 1, 1998; 118(2): 471 - 482.
[Abstract] [Full Text]

Home page
 Microbiol. Mol. Biol. Rev.Home page
M. K. B. Berlyn
Linkage Map of Escherichia coli K-12, Edition 10: The Traditional Map
Microbiol. Mol. Biol. Rev., September 1, 1998; 62(3): 814 - 984.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. V. Lueder and M. A. Phillips
Characterization of Trypanosoma brucei gamma -Glutamylcysteine Synthetase, an Essential Enzyme in the Biosynthesis of Trypanothione (Diglutathionylspermidine)
J. Biol. Chem., July 19, 1996; 271(29): 17485 - 17490.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. A. Fraser, R. D. C. Saunders, and L. I. McLellan
Drosophila melanogaster Glutamate-Cysteine Ligase Activity Is Regulated by a Modifier Subunit with a Mechanism of Action Similar to That of the Mammalian Form
J. Biol. Chem., January 4, 2002; 277(2): 1158 - 1165.
[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.