DOI: 10.1126/science.1184991. Dynamic Regulation of Archaeal Proteasome Gate Opening As Studied by TROSY NMR

Dynamic Regulation of Archaeal Proteasome Gate Opening As Studied by TROSY NMR

10.1126/science.1184991

Crossref journal-article

American Association for the Advancement of Science (AAAS)

Science (221)

Abstract

Open Sesame The proteosome plays a key role in cellular homeostasis through catalyzing protein degradation. It is a barrel-shaped nanomachine whose activity is regulated through gating substrate entry. Religa et al. (p. 98 ) now show that N-terminal gating residues in the proteasome interconvert on a second's time-scale between conformations that place them either outside or inside the proteasomal antechamber. An increase in the number of termini occupying the “in” state decreased rates of hydrolysis. Furthermore, proteasome activators known to increase the proteolysis rate lead to an increase in the number of termini in the “out” state.

Bibliography

Religa, T. L., Sprangers, R., & Kay, L. E. (2010). Dynamic Regulation of Archaeal Proteasome Gate Opening As Studied by TROSY NMR. Science, 328(5974), 98â102.

Authors 3

Tomasz L. Religa (first)
Remco Sprangers (additional)
Lewis E. Kay (additional)

References 29 Referenced 214

Dates

Type	When
Created	15 years, 5 months ago (April 1, 2010, 4:36 p.m.)
Deposited	1 year, 7 months ago (Jan. 10, 2024, 2:56 a.m.)
Indexed	6 days, 12 hours ago (Aug. 30, 2025, 12:50 p.m.)
Issued	15 years, 5 months ago (April 2, 2010)
Published	15 years, 5 months ago (April 2, 2010)
Published Print	15 years, 5 months ago (April 2, 2010)

Funders 0

None

BibTeX

@article{Religa_2010, title={Dynamic Regulation of Archaeal Proteasome Gate Opening As Studied by TROSY NMR}, volume={328}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.1184991}, DOI={10.1126/science.1184991}, number={5974}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Religa, Tomasz L. and Sprangers, Remco and Kay, Lewis E.}, year={2010}, month=apr, pages={98–102} }

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  "abstract": "<jats:title>Open Sesame</jats:title>\n          <jats:p>\n            The proteosome plays a key role in cellular homeostasis through catalyzing protein degradation. It is a barrel-shaped nanomachine whose activity is regulated through gating substrate entry.\n            <jats:bold>\n              Religa\n              <jats:italic>et al.</jats:italic>\n            </jats:bold>\n            (p.\n            <jats:related-article xmlns:xlink=\"http://www.w3.org/1999/xlink\" ext-link-type=\"doi\" page=\"98\" related-article-type=\"in-this-issue\" vol=\"328\" xlink:href=\"10.1126/science.1184991\">98</jats:related-article>\n            ) now show that N-terminal gating residues in the proteasome interconvert on a second's time-scale between conformations that place them either outside or inside the proteasomal antechamber. An increase in the number of termini occupying the \u201cin\u201d state decreased rates of hydrolysis. Furthermore, proteasome activators known to increase the proteolysis rate lead to an increase in the number of termini in the \u201cout\u201d state.\n          </jats:p>",
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