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Shining a light on post‐translational modification
Author(s) -
Nigel G. J. Richards
Publication year - 2008
Publication title -
hfsp journal
Language(s) - English
Resource type - Journals
eISSN - 1955-2068
pISSN - 1955-205X
DOI - 10.2976/1.2889161
Subject(s) - posttranslational modification , glycosylation , computational biology , organelle , function (biology) , protein function , functional diversity , chemistry , computer science , microbiology and biotechnology , biology , biochemistry , gene , enzyme , ecology
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.

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