The genetic code of proteins may dictate much more than their amino acid sequences, a new linkurl:paper;http://www.sciencemag.org/cgi/content/abstract/sci;329/5998/1534?maxtoshow=&hits=10&RESULTFORMAT=&fulltext=Differential+arginylation+of+actin+isoforms+is+regulated+by+coding+sequence-dependent+degradation&searchid=1&FIRSTINDEX=0&resourcetype=HWCIT from __Science__ suggests -- it may hold their ultimate fate.
linkurl:Anna Kashina;http://www.med.upenn.edu/apps/faculty/index.php/g20000546/p4638831 and her colleagues at the University of Pennsylvania described a novel mechanism of protein regulation whereby differences in the mRNA sequences of two nearly identical proteins cause them to be translated into proteins at different speeds. As a result, one form is targeted for quick degradation while the other goes on to carry out important functions in the cell. "It's an innovative piece of work," said Chloë linkurl:Bulinski,;http://www.columbia.edu/cu/biology/faculty-data/chloe-bulinski/faculty.html a cell biologist at Columbia University who was not involved in the study. "It's an example in which two proteins that have different nucleotide sequences but almost the same amino acid sequence can behave very differently." For many years, scientists had been puzzled by the two versions, or isoforms, of...
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β-actin Image:Wikimedia commons |
F. Zhang, et al., "Differential arginylation of actin isoforms is regulated by coding sequence-dependent degradation," Science, 329:1534-37, 2010.
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