Journal Article

PUBDB-2018-05759

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control

Martínez-Lumbreras, S. ; Krysztofinska, E. M. ; Thapaliya, A. ; Spilotros, A. ; Matak-Vinkovic, D. ; Salvadori, E. ; Roboti, P. ; Nyathi, Y. ; Muench, J. H. ; Roessler, M. M. ; Svergun, D. I.EMBL* ; High, S. ; Isaacson, R. L. (Corresponding author)

2018
Springer Heidelberg

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Please use a persistent id in citations: doi:10.1186/s12915-018-0542-3  doi:10.3204/PUBDB-2018-05759

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.

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Contributing Institute(s):

1. EMBL-User (EMBL-User)
2. EMBL (EMBL)

Research Program(s):

1. 6G3 - PETRA III (POF3-622) (POF3-622)

Experiment(s):

1. PETRA Beamline P12 (PETRA III)

Appears in the scientific report 2018

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Database coverage:
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