scholarly journals The kinetics and specificity of cleavage by RNase P is mainly dependent on the structure of the amino acid acceptor stem

1992 ◽  
Vol 20 (3) ◽  
pp. 425-432 ◽  
Author(s):  
Leif A. Kirsebom ◽  
Staffan G. Svärd
Keyword(s):  
Amino Acid ◽  
Rnase P ◽  
Acceptor Stem ◽  
Amino Acid Acceptor

Amino Acid Acceptor Stem of E. coli Suppressor tRNATyr is a Site of Synthetase Recognition

1973 ◽  
Vol 244 (139) ◽  
pp. 261-264 ◽  
Author(s):  
JULIO E. CELIS ◽  
MARTIN L. HOOPER ◽  
JOHN D. SMITH
Keyword(s):  
Amino Acid ◽  
E Coli ◽  
Acceptor Stem ◽  
A Site ◽  
Amino Acid Acceptor

scholarly journals Modification of the amino acid acceptor stem of E. coli tRNAf Met by ligation of chemically synthesized ribooligonucleotides

FEBS Letters ◽  
1985 ◽  
Vol 190 (1) ◽  
pp. 125-128 ◽  
Author(s):  
Takefumi Doi ◽  
Hiroshi Morioka ◽  
Jitsuhiro Matsugi ◽  
Eiko Ohtsuka ◽  
Mono Ikehara
Keyword(s):  
Amino Acid ◽  
E Coli ◽  
Acceptor Stem ◽  
Amino Acid Acceptor

scholarly journals Ribosome Evolution and Structural Capacitance

2019 ◽  
Author(s):  
Ashley M Buckle ◽  
Malcolm Buckle
Keyword(s):  
Amino Acid ◽  
Genetic Code ◽  
Protein Evolution ◽  
Bioinformatic Analysis ◽  
Amino Acid Usage ◽  
Loss Of Function ◽  
Gain Of Function ◽  
Acceptor Stem ◽  
Ribosome Evolution ◽  
Disordered Regions

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.

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