Insights into substrate promiscuity of human seryl-tRNA synthetase.

ABSTRACT: Seryl-tRNA synthetase (SerRS) attaches L-serine to the cognate serine tRNA (tRNA^Ser) and the noncognate selenocysteine tRNA (tRNA^Sec). The latter activity initiates the anabolic cycle of selenocysteine (Sec), proper decoding of an in-frame Sec UGA codon, and synthesis of selenoproteins across all domains of life. While the accuracy of SerRS is important for overall proteome integrity, it is its substrate promiscuity that is vital for the integrity of the selenoproteome. This raises a question as to what elements in the two tRNA species, harboring different anticodon sequences and adopting distinct folds, facilitate aminoacylation by a common aminoacyl-tRNA synthetase. We sought to answer this question by analyzing the ability of human cytosolic SerRS to bind and act o

SUBMITTER: Holman KM 

PROVIDER: S-EPMC5648036 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature