tRNA aminoacylated at high pressure is a correct substrate for protein biosynthesis.
tRNA can be aminoacylated specifically with amino acids at high pressure of 6 kbar (1 bar = 1.013 atm = 0.1 MPa = 10(5) Pa) in the absence of the specific aminoacyl-tRNA synthetase and ATP. In this paper we present new evidence obtained by HPLC chromatography and TLC analysis that the esterification reaction under pressure really takes place at the 3' end of the tRNA molecule. If so, tRNA to be aminoacylated undergoes conformational changes similar to those induced with aminoacyl-tRNA synthetase. The most important finding is that aminoacyl-tRNA obtained at high pressure binds to ribosomes and participates in the synthesis of polyphenylalanine in vitro. This is the best proof of proper charging of tRNA at high pressure.
Institute of Bioorganic Chemistry Polish Academy of Sciences, Poznań, Poland.
A
A
Krzyzaniak
P
P
Sałański
T
T
Twardowski
J
J
Jurczak
J
J
Barciszewski
D000215:Acylation; D000241:Adenosine / Q000737:chemistry; D002851:Chromatography, High Pressure Liquid; D002855:Chromatography, Thin Layer; D004951:Esterification; D010455:Peptides / Q000378:metabolism*; D011312:Pressure; D012360:RNA, Transfer, Phe / Q000737:chemistry* / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000737:chemistry
D010455:Peptides; D012360:RNA, Transfer, Phe; C012001:polyphenylalanine; D000241:Adenosine