Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control.

BMC Biology
Santiago Martínez-LumbrerasRivka L Isaacson

Abstract

Protein quality control mechanisms are essential for cell health and involve delivery of proteins to specific cellular compartments for recycling or degradation. In particular, stray hydrophobic proteins are captured in the aqueous cytosol by a co-chaperone, the small glutamine-rich, tetratricopeptide repeat-containing protein alpha (SGTA), which facilitates the correct targeting of tail-anchored membrane proteins, as well as the sorting of membrane and secretory proteins that mislocalize to the cytosol and endoplasmic reticulum-associated degradation. Full-length SGTA has an unusual elongated dimeric structure that has, until now, evaded detailed structural analysis. The C-terminal region of SGTA plays a key role in binding a broad range of hydrophobic substrates, yet in contrast to the well-characterized N-terminal and TPR domains, there is a lack of structural information on the C-terminal domain. In this study, we present new insights into the conformation and organization of distinct domains of SGTA and show that the C-terminal domain possesses a conserved region essential for substrate processing in vivo. We show that the C-terminal domain region is characterized by α-helical propensity and an intrinsic ability to dimeriz...Continue Reading

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Citations

Apr 27, 2019·Critical Reviews in Biochemistry and Molecular Biology·Jill B GrahamDaniel N Hebert
Feb 22, 2021·The Journal of Biological Chemistry·Ku-Feng LinWilliam M Clemons
Mar 25, 2021·Molecular Brain·Shun KubotaFumiaki Tanaka

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Methods Mentioned

BETA
X-ray
NMR
size-exclusion
dynamic light scattering
FCS
transfections
PCR
gel filtration
size-exclusion chromatography

Software Mentioned

PRIMUS
Metaview
GNOM
GraphPad
SGTA
NMRPipe
GNOM Sample MW
DeerAnalysis2016
TopSpin
SELCON3

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