JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 QUICK SEARCH:   [advanced]


     


A more recent version of this article appeared on May 27, 2005
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
280/21/20740    most recent
M501458200v1
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 Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Zhang, Y.
Right arrow Articles by Gladyshev, V. N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zhang, Y.
Right arrow Articles by Gladyshev, V. N.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print March 22, 2005
J. Biol. Chem, 10.1074/jbc.M501458200
Submitted on February 8, 2005
Revised on March 22, 2005
Accepted on March 22, 2005

Pyrrolysine and selenocysteine use dissimilar decoding strategies

Yan Zhang, Pavel V. Baranov, John F. Atkins, and Vadim N. Gladyshev

Department of Biochemistry, University of Nebraska, Lincoln, NE 68588-0664

Corresponding Author: vgladyshev1{at}unl.edu

Selenocysteine (Sec) and pyrrolysine (Pyl) are known as the 21st and 22nd amino acids in protein. Both are encoded by codons that normally function as stop signals. Sec specification by UGA codons requires the presence of a cis-acting SECIS element. Similarly, it is thought that Pyl is inserted by UAG codons with the help of a putative PYLIS element. Herein, we analyzed the occurrence of Pyl-utilizing organisms, Pyl-associated genes and Pyl-containing proteins. The Pyl trait is restricted to several microbes, and only one organism has both Pyl and Sec. We found that methanogenic archaea that utilize Pyl have few genes that contain in-frame UAG codons, and many of these are followed with nearby UAA or UGA codons. In addition, unambiguous UAG stop signals could not be identified. This bias was not observed in Sec-utilizing organisms and non-Pyl-utilizing archaea, as well as with other stop codons. These observations as well as analyses of the coding potential of UAG codons, overlapping genes and release factor sequences suggest that UAG is not a typical stop signal in Pyl-utilizing archaea. On the other hand, searches for conserved Pyl-containing proteins revealed only four protein families, including methylamine methyltransferases and transposases. Only methylamine methyltransferases matched the Pyl trait and had conserved Pyl, suggesting that this amino acid is used primarily by these enzymes. These findings are best explained by a model wherein UAG codons may have ambiguous meaning and Pyl insertion can effectively compete with translation termination for UAG codons obviating the need for a specific PYLIS structure. Thus, Sec and Pyl follow dissimilar decoding and evolutionary strategies.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Nucleic Acids ResHome page
Y. Zhang and V. N. Gladyshev
High content of proteins containing 21st and 22nd amino acids, selenocysteine and pyrrolysine, in a symbiotic deltaproteobacterium of gutless worm Olavius algarvensis
Nucleic Acids Res., August 1, 2007; 35(15): 4952 - 4963.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
A. Ambrogelly, S. Gundllapalli, S. Herring, C. Polycarpo, C. Frauer, and D. Soll
Pyrrolysine is not hardwired for cotranslational insertion at UAG codons
PNAS, February 27, 2007; 104(9): 3141 - 3146.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
D. G. Longstaff, R. C. Larue, J. E. Faust, A. Mahapatra, L. Zhang, K. B. Green-Church, and J. A. Krzycki
A natural genetic code expansion cassette enables transmissible biosynthesis and genetic encoding of pyrrolysine
PNAS, January 16, 2007; 104(3): 1021 - 1026.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. A. Soares, L. Zhang, R. L. Pitsch, N. M. Kleinholz, R. B. Jones, J. J. Wolff, J. Amster, K. B. Green-Church, and J. A. Krzycki
The Residue Mass of L-Pyrrolysine in Three Distinct Methylamine Methyltransferases
J. Biol. Chem., November 4, 2005; 280(44): 36962 - 36969.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.