Rhomboid intramembrane protease YqgP licenses bacterial membrane protein quality control as adaptor of FtsH AAA protease

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F20%3A00521013" target="_blank" >RIV/61388963:_____/20:00521013 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/20:10411682

Result on the web

<a href="https://www.embopress.org/doi/full/10.15252/embj.2019102935" target="_blank" >https://www.embopress.org/doi/full/10.15252/embj.2019102935</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.15252/embj.2019102935" target="_blank" >10.15252/embj.2019102935</a>

Result language

angličtina

Original language name

Rhomboid intramembrane protease YqgP licenses bacterial membrane protein quality control as adaptor of FtsH AAA protease

Original language description

Magnesium homeostasis is essential for life and depends on magnesium transporters, whose activity and ion selectivity need to be tightly controlled. Rhomboid intramembrane proteases pervade the prokaryotic kingdom, but their functions are largely elusive. Using proteomics, we find that Bacillus subtilis rhomboid protease YqgP interacts with the membrane-bound ATP-dependent processive metalloprotease FtsH and cleaves MgtE, the major high-affinity magnesium transporter in B. subtilis. MgtE cleavage by YqgP is potentiated in conditions of low magnesium and high manganese or zinc, thereby protecting B. subtilis from Mn2+ /Zn2+ toxicity. The N-terminal cytosolic domain of YqgP binds Mn2+ and Zn2+ ions and facilitates MgtE cleavage. Independently of its intrinsic protease activity, YqgP acts as a substrate adaptor for FtsH, a function that is necessary for degradation of MgtE. YqgP thus unites protease and pseudoprotease function, hinting at the evolutionary origin of rhomboid pseudoproteases such as Derlins that are intimately involved in eukaryotic ER-associated degradation (ERAD). Conceptually, the YqgP-FtsH system we describe here is analogous to a primordial form of ″ERAD″ in bacteria and exemplifies an ancestral function of rhomboid-superfamily proteins.

Czech name

—

Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2020

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

EMBO Journal

ISSN

0261-4189

e-ISSN

1460-2075

Volume of the periodical

39

Issue of the periodical within the volume

10

Country of publishing house

GB - UNITED KINGDOM

Number of pages

19

Pages from-to

e102935

UT code for WoS article

000506708200001

EID of the result in the Scopus database

2-s2.0-85078045327