scholarly journals Codon and Amino Acid Usage Are Shaped by Selection Across Divergent Model Organisms of the Pancrustacea

2015 ◽  
Vol 5 (11) ◽  
pp. 2307-2321 ◽  
Author(s):  
Carrie A. Whittle ◽  
Cassandra G. Extavour
Genetics ◽  
2003 ◽  
Vol 164 (4) ◽  
pp. 1291-1303 ◽  
Author(s):  
Hiroshi Akashi

AbstractThe primary structures of peptides may be adapted for efficient synthesis as well as proper function. Here, the Saccharomyces cerevisiae genome sequence, DNA microarray expression data, tRNA gene numbers, and functional categorizations of proteins are employed to determine whether the amino acid composition of peptides reflects natural selection to optimize the speed and accuracy of translation. Strong relationships between synonymous codon usage bias and estimates of transcript abundance suggest that DNA array data serve as adequate predictors of translation rates. Amino acid usage also shows striking relationships with expression levels. Stronger correlations between tRNA concentrations and amino acid abundances among highly expressed proteins than among less abundant proteins support adaptation of both tRNA abundances and amino acid usage to enhance the speed and accuracy of protein synthesis. Natural selection for efficient synthesis appears to also favor shorter proteins as a function of their expression levels. Comparisons restricted to proteins within functional classes are employed to control for differences in amino acid composition and protein size that reflect differences in the functional requirements of proteins expressed at different levels.


Author(s):  
Ashley M Buckle ◽  
Malcolm Buckle

In addition to the canonical loss-of-function mutations, mutations in proteins may additionally result in gain-of-function through the binary activation of cryptic ‘structural capacitance elements’. Our previous bioinformatic analysis allowed us to propose a new mechanism of protein evolution - structural capacitance – that arises via the generation of new elements of microstructure upon mutations that cause a disorder-to-order (DO) transition in previously disordered regions of proteins. Here we propose that the DO transition is a necessary follow-on from expected early codon-anticodon and tRNA acceptor stem-amino acid usage, via the accumulation of structural capacitance elements - reservoirs of disorder in proteins. We develop this argument further to posit that structural capacitance is an inherent consequence of the evolution of the genetic code.


Gene ◽  
2003 ◽  
Vol 311 ◽  
pp. 35-42 ◽  
Author(s):  
Rickard Sandberg ◽  
Carl-Ivar Bränden ◽  
Ingemar Ernberg ◽  
Joakim Cöster

PLoS ONE ◽  
2014 ◽  
Vol 9 (10) ◽  
pp. e110381 ◽  
Author(s):  
Yousheng Rao ◽  
Zhangfeng Wang ◽  
Xuewen Chai ◽  
Qinghua Nie ◽  
Xiquan Zhang
Keyword(s):  

1991 ◽  
Vol 19 (22) ◽  
pp. 6119-6122 ◽  
Author(s):  
Fumiaki Yamao ◽  
Yoshiki Andachi ◽  
Akira Muto ◽  
Toshimichi Ikemura ◽  
Syozo Osawa

1989 ◽  
Vol 65 (4) ◽  
pp. 73-75 ◽  
Author(s):  
Fumiaki YAMAO ◽  
Yoshiki ANDACHI ◽  
Akira MUTO ◽  
Toshimichi IKEMURA ◽  
Syozo OSAWA

Genetica ◽  
2017 ◽  
Vol 146 (1) ◽  
pp. 13-27 ◽  
Author(s):  
Shilpee Pal ◽  
Indrani Sarkar ◽  
Ayan Roy ◽  
Pradeep K. Das Mohapatra ◽  
Keshab C. Mondal ◽  
...  

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