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Accumulation of the Type IV prepilin triggers degradation of SecY and YidC and inhibits synthesis of Photosystem II proteins in the cyanobacterium Synechocystis PCC 6803
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SYSNO ASEP 0441078 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Accumulation of the Type IV prepilin triggers degradation of SecY and YidC and inhibits synthesis of Photosystem II proteins in the cyanobacterium Synechocystis PCC 6803 Author(s) Linhartová, Markéta (MBU-M) RID, ORCID
Bučinská, Lenka (MBU-M) RID
Halada, Petr (MBU-M) RID, ORCID
Ječmen, T. (CZ)
Šetlík, Jiří (MBU-M)
Komenda, Josef (MBU-M) RID, ORCID
Sobotka, Roman (MBU-M) RID, ORCIDNumber of authors 7 Source Title Molecular Microbiology - ISSN 0950-382X
Roč. 93, č. 6 (2014), s. 1207-1223Number of pages 16 s. Language eng - English Country GB - United Kingdom Keywords prepilin ; cab-like proteins ; Synechocystit Subject RIV EE - Microbiology, Virology R&D Projects CZ.2.16/3.1.00/24023 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GA14-13967S GA ČR - Czech Science Foundation (CSF) Institutional support MBU-M - RVO:61388971 UT WOS 000342757200011 Annotation Type IV pilins are bacterial proteins that are small in size but have a broad range of functions, including motility, transformation competence and secretion. Although pilins vary in sequence, they possess a characteristic signal peptide that has to be removed by the prepilin peptidase PilD during pilin maturation. We generated a pilD (slr1120) null mutant of the cyanobacterium Synechocystis 6803 that accumulates an unprocessed form of the major pilin PilA1 (pPilA1) and its non-glycosylated derivative (NpPilA1). Notably, the pilD strain had aberrant membrane ultrastructure and did not grow photoautotrophically because the synthesis of Photosystem II subunits was abolished. However, other membrane components such as Photosystem I and ATP synthase were synthesized at levels comparable to the control strain. Proliferation of the pilD strain was rescued by elimination of the pilA1 gene, demonstrating that PilA1 prepilin inhibited the synthesis of Photosystem II. Furthermore, NpPilA1 co-immunoprecipitated with the SecY translocase and the YidC insertase, and both of these essential translocon components were degraded in the mutant. We propose that unprocessed prepilins inactivate an identical pool of translocons that function in the synthesis of both pilins and the core subunits of Photosystem II. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2015
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