umu.sePublications
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
Protease gene families in Populus and Arabidopsis
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).ORCID iD: 0000-0002-7906-6891
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
2006 (English)In: BMC Plant Biology, ISSN 1471-2229, Vol. 6, no 30, 1-24 p.Article in journal (Refereed) Published
Abstract [en]

Proteases play key roles in plants, maintaining strict protein quality control and degrading specific sets of proteins in response to diverse environmental and developmental stimuli. Similarities and differences between the proteases expressed in different species may give valuable insights into their physiological roles and evolution. RESULTS: We have performed a comparative analysis of protease genes in the two sequenced dicot genomes, Arabidopsis thaliana and Populus trichocarpa by using genes coding for proteases in the MEROPS database 1 for Arabidopsis to identify homologous sequences in Populus. A multigene-based phylogenetic analysis was performed. Most protease families were found to be larger in Populus than in Arabidopsis, reflecting recent genome duplication. Detailed studies on e.g. the DegP, Clp, FtsH, Lon, rhomboid and papain-Like protease families showed the pattern of gene family expansion and gene loss was complex. We finally show that different Populus tissues express unique suites of protease genes and that the mRNA levels of different classes of proteases change along a developmental gradient. CONCLUSION: Recent gene family expansion and contractions have made the Arabidopsis and Populus complements of proteases different and this, together with expression patterns, gives indications about the roles of the individual gene products or groups of proteases.

Place, publisher, year, edition, pages
2006. Vol. 6, no 30, 1-24 p.
Identifiers
URN: urn:nbn:se:umu:diva-10870DOI: doi:10.1186/1471-2229-6-30PubMedID: 17181860OAI: oai:DiVA.org:umu-10870DiVA: diva2:150541
Available from: 2008-04-03 Created: 2008-04-03 Last updated: 2015-04-29Bibliographically approved
In thesis
1. The Role of Proteases in Plant Development
Open this publication in new window or tab >>The Role of Proteases in Plant Development
2007 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Proteases play key roles in plants, maintaining strict protein quality control and degrading specific sets of proteins in response to diverse environmental and developmental stimuli. Similarities and differences between the proteases expressed in different species may give valuable insights into their physiological roles and evolution.

Systematic comparative analysis of the available sequenced genomes of two model organisms led to the identification of an increasing number of protease genes, giving insights about protein sequences that are conserved in the different species, and thus are likely to have common functions in them and the acquisition of new genes, elucidate issues concerning non-functionalization, neofunctionalization and subfunctionalization.

The involvement of proteases in senescence and PCD was investigated. While PCD in woody tissues shows the importance of vacuole proteases in the process, the senescence in leaves demonstrate to be a slower and more ordered mechanism starting in the chloroplast where the proteases there localized become important.

The light-harvesting complex of Photosystem II is very susceptible to protease attack during leaf senescence. We were able to show that a metallo-protease belonging to the FtsH family is involved on the process in vitro. Arabidopsis knockout mutants confirmed the function of FtsH6 in vivo.

Place, publisher, year, edition, pages
Umeå: Kemi, 2007. 45 p.
Keyword
Comparative genomics, protease, PCD, leaf senescence, FtsH, Arabidopsis, Populus
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-1386 (URN)978-91-7264-422-9 (ISBN)
Public defence
2007-10-26, KB3B1, KBC-huset, Linnaeus V. 6, Umeå, 13:00 (English)
Opponent
Supervisors
Available from: 2007-10-05 Created: 2007-10-05 Last updated: 2009-09-08Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Authority records BETA

Jansson, StefanFunk, Christiane

Search in DiVA

By author/editor
Jansson, StefanFunk, Christiane
By organisation
Department of ChemistryDepartment of Plant PhysiologyUmeå Plant Science Centre (UPSC)
In the same journal
BMC Plant Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 85 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