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Mutations Suppressing the Lack of Prepilin Peptidase Provide Insights Into the Maturation of the Major Pilin Protein in Cyanobacteria
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SYSNO ASEP 0548423 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Mutations Suppressing the Lack of Prepilin Peptidase Provide Insights Into the Maturation of the Major Pilin Protein in Cyanobacteria Author(s) Linhartová, Markéta (MBU-M) RID, ORCID
Skotnicová, Petra (MBU-M) ORCID, RID
Hakkila, K. (FI)
Tichý, Martin (MBU-M) RID
Komenda, Josef (MBU-M) RID, ORCID
Knoppová, Jana (MBU-M) RID
Gilabert, J. F. (ES)
Guallar, V. (ES)
Tyystjaervi, T. (FI)
Sobotka, Roman (MBU-M) RID, ORCIDArticle number 756912 Source Title Frontiers in Microbiology. - : Frontiers Research Foundation - ISSN 1664-302X
Roč. 12, OCT 12 2021 (2021)Number of pages 14 s. Language eng - English Country CH - Switzerland Keywords Type IV pili ; Synechocystis ; photosystem II ; PilD peptidase ; suppressor mutations Subject RIV EE - Microbiology, Virology OECD category Microbiology R&D Projects GX19-29225X GA ČR - Czech Science Foundation (CSF) Method of publishing Open access Institutional support MBU-M - RVO:61388971 UT WOS 000713450800001 EID SCOPUS 85117896071 DOI 10.3389/fmicb.2021.756912 Annotation Type IV pili are bacterial surface-exposed filaments that are built up by small monomers called pilin proteins. Pilins are synthesized as longer precursors (prepilins), the N-terminal signal peptide of which must be removed by the processing protease PilD. A mutant of the cyanobacterium Synechocystis sp. PCC 6803 lacking the PilD protease is not capable of photoautotrophic growth because of the impaired function of Sec translocons. Here, we isolated phototrophic suppressor strains of the original Delta pilD mutant and, by sequencing their genomes, identified secondary mutations in the SigF sigma factor, the gamma subunit of RNA polymerase, the signal peptide of major pilin PilA1, and in the pilA1-pilA2 intergenic region. Characterization of suppressor strains suggests that, rather than the total prepilin level in the cell, the presence of non-glycosylated PilA1 prepilin is specifically harmful. We propose that the restricted lateral mobility of the non-glycosylated PilA1 prepilin causes its accumulation in the translocon-rich membrane domains, which attenuates the synthesis of membrane proteins./p Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2022 Electronic address https://www.frontiersin.org/articles/10.3389/fmicb.2021.756912/full
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