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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

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Published on: October 4, 2017

Structural basis for tRNA-dependent cysteine biosynthesis.

Meirong Chen¹, Koji Kato^1,2, Yume Kubo¹

¹Graduate School of Life Science, Hokkaido University, Sapporo, 060-0810, Japan.

Nature Communications

|November 17, 2017

Summary

This summary is machine-generated.

A novel ternary complex, the transsulfursome, facilitates cysteine biosynthesis through tRNA-dependent mechanisms. This complex, involving SepRS, SepCysS, and SepCysE proteins, ensures efficient and accurate synthesis of cysteine for the genetic code.

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Cysteine biosynthesis occurs via a two-step indirect tRNA-dependent pathway.
O-phosphoseryl-tRNA synthetase (SepRS) and Sep-tRNA:Cys-tRNA synthase (SepCysS) are key enzymes.
In ancestral methanogens, SepCysE forms a ternary complex, the transsulfursome, with SepRS and SepCysS.

Purpose of the Study:

To elucidate the structural basis and mechanism of the transsulfursome.
To understand how SepCysE mediates tRNA^Cys channeling between SepRS and SepCysS.
To explore the implications for cysteine biosynthesis and its evolutionary origin.

Main Methods:

X-ray crystallography
Small-angle X-ray scattering (SAXS)
Electron microscopy (EM)
Biochemical assays

Main Results:

The three domains of SepCysE bind SepRS, SepCysS, and tRNA^Cys respectively.
SepCysE mediates the dynamic architecture of the transsulfursome.
Long-range channeling of tRNA^Cys between distant active sites of SepRS and SepCysS is enabled.

Conclusions:

The transsulfursome facilitates efficient and accurate tRNA-dependent cysteine biosynthesis.
This channeling mechanism prevents translational fidelity challenges.
The findings suggest a potential mechanism for the original incorporation of cysteine into the genetic code.