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Phylogenetic distribution and diversity of bacterial pseudo-orthocaspases underline their putative role in photosynthesis
Umea Univ, Dept Chem, Umea, Sweden. emencic, Marina; Dolinar, Marko.
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science, Systems Biology. KTH, Centres, Science for Life Laboratory, SciLifeLab.
2019 (English)In: Frontiers in Plant Science, ISSN 1664-462X, E-ISSN 1664-462X, Vol. 10, article id 293Article in journal (Refereed) Published
Abstract [en]

Orthocaspases are prokaryotic caspase homologs – proteases, which cleave their substrates after positively charged residues using a conserved histidine – cysteine (HC) dyad situated in a catalytic p20 domain. However, in orthocaspases pseudo-variants have been identified, which instead of the catalytic HC residues contain tyrosine and serine, respectively. The presence and distribution of these presumably proteolytically inactive p20-containing enzymes has until now escaped attention. We have performed a detailed analysis of orthocaspases in all available prokaryotic genomes, focusing on pseudo-orthocaspases. Surprisingly we identified type I metacaspase homologs in filamentous cyanobacteria. While genes encoding pseudo-orthocaspases seem to be absent in Archaea, our results show conservation of these genes in organisms performing either anoxygenic photosynthesis (orders Rhizobiales, Rhodobacterales, and Rhodospirillales in Alphaproteobacteria) or oxygenic photosynthesis (all sequenced cyanobacteria, except Gloeobacter, Prochlorococcus, and Cyanobium). Contrary to earlier reports, we were able to detect pseudo-orthocaspases in all sequenced strains of the unicellular cyanobacteria Synechococcus and Synechocystis. In silico comparisons of the primary as well as tertiary structures of pseudo-p20 domains with their presumably proteolytically active homologs suggest that differences in their amino acid sequences have no influence on the overall structures. Mutations therefore affect most likely only the proteolytic activity. Our data provide an insight into diversification of pseudo-orthocaspases in Prokaryotes, their taxa-specific distribution, and allow suggestions on their taxa-specific function.

Place, publisher, year, edition, pages
FRONTIERS MEDIA SA , 2019. Vol. 10, article id 293
Keywords [en]
orthocaspase, metacaspase, photosynthesis, pseudo-enzyme, cyanobacteria
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-248072DOI: 10.3389/fpls.2019.00293ISI: 000461133100001Scopus ID: 2-s2.0-85064233837OAI: oai:DiVA.org:kth-248072DiVA, id: diva2:1314668
Note

QC 20190509

Available from: 2019-05-09 Created: 2019-05-09 Last updated: 2019-05-09Bibliographically approved

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