Abstract
In the presence of purified Escherichia coli lysyl-tRNA synthetase [L-lysine:tRNALys ligase (AMP-forming) EC 6.1.1.6], L-lysine, and ATP, addition of the nucleotide ppGpp results in formation of a unique product-A(5')ppp(5') Gpp. The same compound is also formed very rapidly in a cell-free protein-synthesizing system when ppGpp is added. The possible significance of this reaction in the rapid turnover of ppGpp and as a more general mechanism by which an AMP residue is activated and introduced onto a 5'-diphosphorylated species, including the 5'-end of an RNA, is further discussed.
MeSH Terms
Adenine Nucleotides/metabolism
Adenosine Triphosphate/metabolism
Alkaline Phosphatase
Avian Myeloblastosis Virus/metabolism
Bacterial Proteins/biosynthesis
Chromatography, DEAE-Cellulose
Chromatography, Thin Layer
Escherichia coli/metabolism
Guanine Nucleotides/metabolism
Lysine-tRNA Ligase/metabolism
Phosphoric Diester Hydrolases
Protein Biosynthesis
RNA, Viral/metabolism
Snake Venoms
Transfer RNA Aminoacylation
Chemicals
Adenine Nucleotides
Bacterial Proteins
Guanine Nucleotides
RNA, Viral
Snake Venoms
Adenosine Triphosphate
Alkaline Phosphatase
Phosphoric Diester Hydrolases
Lysine-tRNA Ligase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Rapaport E
Svihovec S K
Zamecnik P C
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20 references, click to expand
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