Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Structural and functional diversity of caspase homologues in non-metazoan organisms
Umeå University, Faculty of Science and Technology, Department of Chemistry. Department of Chemistry and Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, Večna pot 113, 1000 Ljubljana, Slovenia.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
2018 (English)In: Protoplasma, ISSN 0033-183X, E-ISSN 1615-6102, Vol. 255, no 1, p. 387-397Article, review/survey (Refereed) Published
Abstract [en]

Caspases, the proteases involved in initiation and execution of metazoan programmed cell death, are only present in animals, while their structural homologues can be found in all domains of life, spanning from simple prokaryotes (orthocaspases) to yeast and plants (metacaspases). All members of this wide protease family contain the p20 domain, which harbours the catalytic dyad formed by the two amino acid residues, histidine and cysteine. Despite the high structural similarity of the p20 domain, metacaspases and orthocaspases were found to exhibit different substrate specificities than caspases. While the former cleave their substrates after basic amino acid residues, the latter accommodate substrates with negative charge. This observation is crucial for the re-evaluation of non-metazoan caspase homologues being involved in processes of programmed cell death. In this review, we analyse the structural diversity of enzymes containing the p20 domain, with focus on the orthocaspases, and summarise recent advances in research of orthocaspases and metacaspases of cyanobacteria, algae and higher plants. Although caspase homologues were initially proposed to be involved in execution of cell death, accumulating evidence supports the role of metacaspases and orthocaspases as important contributors to cell homeostasis during normal physiological conditions or cell differentiation and ageing.

Place, publisher, year, edition, pages
Springer Publishing Company, 2018. Vol. 255, no 1, p. 387-397
Keyword [en]
Algae, Cyanobacteria, Cell death, Cysteine protease, Metacaspase, Orthocaspase
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-143703DOI: 10.1007/s00709-017-1145-5ISI: 000419461400028OAI: oai:DiVA.org:umu-143703DiVA, id: diva2:1171485
Available from: 2018-01-08 Created: 2018-01-08 Last updated: 2018-03-26Bibliographically approved

Open Access in DiVA

fulltext(5702 kB)15 downloads
File information
File name FULLTEXT01.pdfFile size 5702 kBChecksum SHA-512
19b4ca87ae1dc68a481f46ae3ba26093c78028d27cb970a9f8570c9df7e24c3653c8fb88829d44e373685f25eacea12410c06bc7d29519069ec43b6ca62a1694
Type fulltextMimetype application/pdf

Other links

Publisher's full text

Search in DiVA

By author/editor
Klemenčič, MarinaFunk, Christiane
By organisation
Department of Chemistry
In the same journal
Protoplasma
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar
Total: 15 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 40 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf