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2017 ; 8
(1
): 1521
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Structural basis for tRNA-dependent cysteine biosynthesis
#MMPMID29142195
Chen M
; Kato K
; Kubo Y
; Tanaka Y
; Liu Y
; Long F
; Whitman WB
; Lill P
; Gatsogiannis C
; Raunser S
; Shimizu N
; Shinoda A
; Nakamura A
; Tanaka I
; Yao M
Nat Commun
2017[Nov]; 8
(1
): 1521
PMID29142195
show ga
Cysteine can be synthesized by tRNA-dependent mechanism using a two-step indirect
pathway, where O-phosphoseryl-tRNA synthetase (SepRS) catalyzes the ligation of a
mismatching O-phosphoserine (Sep) to tRNA(Cys) followed by the conversion of
tRNA-bounded Sep into cysteine by Sep-tRNA:Cys-tRNA synthase (SepCysS). In
ancestral methanogens, a third protein SepCysE forms a bridge between the two
enzymes to create a ternary complex named the transsulfursome. By combination of
X-ray crystallography, SAXS and EM, together with biochemical evidences, here we
show that the three domains of SepCysE each bind SepRS, SepCysS, and tRNA(Cys),
respectively, which mediates the dynamic architecture of the transsulfursome and
thus enables a global long-range channeling of tRNA(Cys) between SepRS and
SepCysS distant active sites. This channeling mechanism could facilitate the
consecutive reactions of the two-step indirect pathway of Cys-tRNA(Cys) synthesis
(tRNA-dependent cysteine biosynthesis) to prevent challenge of translational
fidelity, and may reflect the mechanism that cysteine was originally added into
genetic code.
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