Skip Navigation

This Article
Right arrow Print PDF (472K)
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 (37)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Baldacci, G.
Right arrow Articles by de Recondo, A.-M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Baldacci, G.
Right arrow Articles by de Recondo, A.-M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1990, Vol. 18, No. 3 507-511
© 1990

MOLECULAR BIOLOGY

Functional implications related to the gene structure of the elongation factor EF-Tu from Halobacterium marismortui

Giuseppe Baldacci, Françoise Guinet1,*, Jeanne Tillit, Giuseppe Zaccai2 and Anne-Marie de Recondo

GBGM, CNRS UPR 272, 94802 Villejuif Cedex, France 1EMBL, Grenoble outstation, 156X, 38042 Grenoble Cedex, France 2ILL, CNRS URA 1333, 156X, 38042 Grenoble Cedex, France

Received October 23, 1989. Accepted November 29, 1989.

The primary structure of the gene for the elongation factor EF-Tu from the halophilic archaebacterium Halobacterium marismortui (hEF-Tu) is described. It is the first gene of a halophilic elongation factor EF-Tu to be sequenced. When the sequence of hEF-Tu is compared to that of homologous proteins from other organisms, the highest identity (61%) is found with EF-Tu from Methanococcus vannielii, a non-halophilic archaebacterium. In the search for halophilic characteristics therefore the most appropriate comparison is with the M. vannielii sequence. The excess of acidic amino acid residues in the hEF-Tu sequence (already observed in the composition of other halophilic proteins) results to a large extent from changes of Lys, Asn or Gin to Asp or Glu. A structural analysis algorithm applied to the halophilic sequence places these acidic residues on the surface of the protein. The corresponding residues in the crystal structure of the first domain of EF-Tu from E. coli (the only EF-Tu structure available) are grouped in patches on the protein surface, in each of which several residues that may be far apart in the sequence come quite close to each other in the tertiary structure.

* Present address: Rhone-Poulenc Santé, IBV, 13 Quai J.Guesde 94400 Vitry sur Seine, France


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. Biol. Chem.Home page
K. L. Britton, T. J. Stillman, K. S. P. Yip, P. Forterre, P. C. Engel, and D. W. Rice
Insights into the Molecular Basis of Salt Tolerance from the Study of Glutamate Dehydrogenase from Halobacterium salinarum
J. Biol. Chem., April 10, 1998; 273(15): 9023 - 9030.
[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.