Literature DB >> 19404471

Shining a light on post-translational modification.

Nigel G J Richards1.   

Abstract

Post-translational modification, such as phosphorylation or glycosylation, provides a mechanism for increasing the diversity of protein structures in the cell and regulating biological activity. In addition, such modifications may result in the localization of proteins to specific cellular organelles, with incorrect targeting being associated with a number of diseases. The simplest strategy to identify the functional importance of post-translational modifications is to use mutagenesis methods to replace the residue that is post-translationally modified by one that cannot undergo the relevant chemical transformation. Merely causing "loss of function" does not, however, address questions concerning how cellular function depends on the timing of post-translational changes andor the movement of modified proteins between organelles. The recent demonstration that genetically encoded "photocaged" proteins can be employed to resolve such issues therefore represents an exciting advance in this research area, and is an elegant illustration of the power of combining the power of chemical synthesis and methods for manipulating the biological machinery of protein synthesis.

Year:  2008        PMID: 19404471      PMCID: PMC2645574          DOI: 10.2976/1.2889161

Source DB:  PubMed          Journal:  HFSP J        ISSN: 1955-205X


  13 in total

1.  Roles of phosphorylation sites in regulating activity of the transcription factor Pho4.

Authors:  A Komeili; E K O'Shea
Journal:  Science       Date:  1999-05-07       Impact factor: 47.728

2.  Structural and mechanistic basis of pre- and posttransfer editing by leucyl-tRNA synthetase.

Authors:  Tommie L Lincecum; Michael Tukalo; Anna Yaremchuk; Richard S Mursinna; Amy M Williams; Brian S Sproat; Wendy Van Den Eynde; Andreas Link; Serge Van Calenbergh; Morten Grøtli; Susan A Martinis; Stephen Cusack
Journal:  Mol Cell       Date:  2003-04       Impact factor: 17.970

Review 3.  The preparation and in vivo applications of caged peptides and proteins.

Authors:  David S Lawrence
Journal:  Curr Opin Chem Biol       Date:  2005-09-22       Impact factor: 8.822

4.  A genetically encoded photocaged tyrosine.

Authors:  Alexander Deiters; Dan Groff; Youngha Ryu; Jianming Xie; Peter G Schultz
Journal:  Angew Chem Int Ed Engl       Date:  2006-04-21       Impact factor: 15.336

5.  Regulation of PHO4 nuclear localization by the PHO80-PHO85 cyclin-CDK complex.

Authors:  E M O'Neill; A Kaffman; E R Jolly; E K O'Shea
Journal:  Science       Date:  1996-01-12       Impact factor: 47.728

6.  Phosphorylation of the transcription factor PHO4 by a cyclin-CDK complex, PHO80-PHO85.

Authors:  A Kaffman; I Herskowitz; R Tjian; E K O'Shea
Journal:  Science       Date:  1994-02-25       Impact factor: 47.728

Review 7.  The phosphatase system in Saccharomyces cerevisiae.

Authors:  Y Oshima
Journal:  Genes Genet Syst       Date:  1997-12       Impact factor: 1.517

8.  Control of protein phosphorylation with a genetically encoded photocaged amino acid.

Authors:  Edward A Lemke; Daniel Summerer; Bernhard H Geierstanger; Scott M Brittain; Peter G Schultz
Journal:  Nat Chem Biol       Date:  2007-10-28       Impact factor: 15.040

9.  A new approach to time-resolved studies of ATP-requiring biological systems; laser flash photolysis of caged ATP.

Authors:  J A McCray; L Herbette; T Kihara; D R Trentham
Journal:  Proc Natl Acad Sci U S A       Date:  1980-12       Impact factor: 11.205

Review 10.  Synthetic biology.

Authors:  Steven A Benner; A Michael Sismour
Journal:  Nat Rev Genet       Date:  2005-07       Impact factor: 53.242

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