Skip Navigation

This Article
Right arrow Print PDF (4242K)
Right arrow An erratum has been published
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 (31)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Borel, F.
Right arrow Articles by Härtlein, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Borel, F.
Right arrow Articles by Härtlein, M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1994, Vol. 22, No. 15 2963-2969
© 1994

ENZYMOLOGY

Seryl-tRNA synthetase from Escherichia coli: implication of its N-terminal domain in aminoacylation activity and specificity

Franck Borel, Christine Vincent, Reuben Leberman and Michael Härtlein*

European Molecular Biology Laboratory, Grenoble Outstation BP 156, 38042 Grenoble Cedex 9, France

*To whom correspondence should be addressed

Received April 18, 1994. Revised July 7, 1994. Accepted July 7, 1994.

Escherichia coli seryl-tRNA synthetase (SerRS) a dimeric class II aminoacyl-tRNA synthetase with two structural domains charges specifically the five isoacceptor tRNAser as well as the tRNAsec (selC product) of E.coli. The N-terminal domain is a 60 A long armlike coiled coil structure built of 2 long antiparallel a-h helices, whereas the C-terminal domain is a {alpha}-ß structure. A deletion of the N-terminal arm of the enzyme does not affect the amino acid activation step of the reaction, but reduces dramatically aminoacylation activity. The KcatIKm value for the mutant enzyme is reduced by more than 4 orders of magnitude, with a nearly 30 fold increased Km value for tRNAser. An only slightly truncated mutant form (16 amino acids of the tip of the arm replaced by a glycine) has an intermediate aminoacylation activity. Both mutant synthetases have lost their specificity for tRNAser and charge also non-cognate type 1 tRNA(s). Our results support the hypothesis that class II synthetases have evolved from an ancestral catalytic core enzyme by adding non-catalytic N-terminal or C-terminal tRNA binding (specificity) domains which act as determinants for cognate and anti-determinants for non-cognate tRNAs.


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
S. Bilokapic, N. Ivic, V. Godinic-Mikulcic, I. Piantanida, N. Ban, and I. Weygand-Durasevic
Idiosyncratic Helix-Turn-Helix Motif in Methanosarcina barkeri Seryl-tRNA Synthetase Has a Critical Architectural Role
J. Biol. Chem., April 17, 2009; 284(16): 10706 - 10713.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. Geslain, E. Aeby, T. Guitart, T. E. Jones, M. C. de Moura, F. Charriere, A. Schneider, and L. R. de Pouplana
Trypanosoma Seryl-tRNA Synthetase Is a Metazoan-like Enzyme with High Affinity for tRNASec
J. Biol. Chem., December 15, 2006; 281(50): 38217 - 38225.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Takita and K. Inouye
Transition State Stabilization by the N-terminal Anticodon-binding Domain of Lysyl-tRNA Synthetase
J. Biol. Chem., August 2, 2002; 277(32): 29275 - 29282.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B. Lenhard, B. Lenhard, I. Landeka, and D. Soll
Defining the Active Site of Yeast Seryl-tRNA Synthetase. MUTATIONS IN MOTIF 2LOOP RESIDUES AFFECT tRNA-DEPENDENT AMINO ACID RECOGNITION
J. Biol. Chem., January 10, 1997; 272(2): 1136 - 1141.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
I. Weygand-Durasevic, B. Lenhard, S. Filipic, and D. Söll
The C-terminal Extension of Yeast Seryl-tRNA Synthetase Affects Stability of the Enzyme and Its Substrate Affinity
J. Biol. Chem., February 2, 1996; 271(5): 2455 - 2461.
[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.