scholarly journals The tRNA levels in bacterial cells as affected by amino acid usage in proteins.

1989 ◽  
Vol 65 (4) ◽  
pp. 73-75 ◽  
Author(s):  
Fumiaki YAMAO ◽  
Yoshiki ANDACHI ◽  
Akira MUTO ◽  
Toshimichi IKEMURA ◽  
Syozo OSAWA
1991 ◽  
Vol 19 (22) ◽  
pp. 6119-6122 ◽  
Author(s):  
Fumiaki Yamao ◽  
Yoshiki Andachi ◽  
Akira Muto ◽  
Toshimichi Ikemura ◽  
Syozo Osawa

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

1983 ◽  
Vol 40 (S2) ◽  
pp. s215-s220 ◽  
Author(s):  
A. Foda ◽  
J. H. Vandermeulen ◽  
J. J. Wrench

Bio-conversion of Se was examined by incubating Pseudomonas marina in seawater containing either selenite (Na2SeIVO3) or selenate (Na2SeVIO4). At the concentrations of selenite and selenate used (10−4–10−7 mol/L), the growth of P. marina was not inhibited. Under these conditions, selenite was taken up by P. marina, but selenate was not found to enter the cells. Pseudomonas marina incorporated selenite from filtered seawater into sub-cellular fractions, primarily protein (30–50%) and amino acids (44–70%). When incubated in marine broth, P. marina incorporated 75selenite primarily into protein (up to 75%), with a lesser amount into the amino acid fraction (approximately 25%). Insignificant amounts were associated with the bacterial lipid fraction. SeIV was found in the protein and amino acid fractions within 10 min of incubation in medium containing selenite. In uptake studies the level of SeIV in the incubating medium decreased markedly, corresponding presumably to SeIV entering the bacterial cells from the medium. However, simultaneous measurements of total Se in the medium (gas–liquid chromatography following photooxidation) revealed an increasing amount of non-SeIV species of Se in the medium throughout the same period. These results were interpreted as due to the bioconversion of selenite by P. marina into water-soluble non-SeIV metabolite(s) and their subsequent release back into the medium. Up to 35% of the total Se found in the medium after 24 h can be accounted for by this conversion of SeIV into another oxidation state. Pseudomonas marina is also capable of reducing SeIV to elemental Se; this pathway becomes increasingly evident at higher concentrations of Na2SeO3.


1992 ◽  
Vol 281 (3) ◽  
pp. 157-161 ◽  
Author(s):  
Giorgio Brandi ◽  
Lorena Luzzi ◽  
Paolo Giacomoni ◽  
Amedeo Albano ◽  
Flaminio Cattabeni ◽  
...  

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