Change search
ReferencesLink to record
Permanent link

Direct link
Insights into the Cyanobacterial Deg/HtrA Proteases
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
2016 (English)In: Frontiers in Plant Science, ISSN 1664-462X, E-ISSN 1664-462X, Vol. 7, 694Article in journal (Refereed) PublishedText
Abstract [en]

Proteins are the main machinery for all living processes in a cell; they provide structural elements, regulate biochemical reactions as enzymes, and are the interface to the outside as receptors and transporters. Like any other machinery proteins have to be assembled correctly and need maintenance after damage, e.g., caused by changes in environmental conditions, genetic mutations, and limitations in the availability of cofactors. Proteases and chaperones help in repair, assembly, and folding of damaged and misfolded protein complexes cost-effective, with low energy investment compared with neo-synthesis. Despite their importance for viability, the specific biological role of most proteases in vivo is largely unknown. Deg/HtrA proteases, a family of serinetype ATP-independent proteases, have been shown in higher plants to be involved in the degradation of the Photosystem II reaction center protein D1. The objective of this review is to highlight the structure and function of their cyanobacterial orthologs. Homology modeling was used to find specific features of the SynDeg/HtrA proteases of Synechocystis sp. PCC 6803. Based on the available data concerning their location and their physiological substrates we conclude that these Deg proteases not only have important housekeeping and chaperone functions within the cell, but also are needed for remodeling the cell exterior.

Place, publisher, year, edition, pages
Frontiers Media S.A , 2016. Vol. 7, 694
Keyword [en]
cyanobacteria, serine proteases, phylogeny, PSII degradation, chaperone, secretion, cell surface
National Category
Chemical Sciences Biochemistry and Molecular Biology
URN: urn:nbn:se:umu:diva-121359DOI: 10.3389/fpls.2016.00694ISI: 000376743000001OAI: diva2:932248
Available from: 2016-06-01 Created: 2016-06-01 Last updated: 2016-08-11Bibliographically approved

Open Access in DiVA

fulltext(1670 kB)13 downloads
File information
File name FULLTEXT01.pdfFile size 1670 kBChecksum SHA-512
Type fulltextMimetype application/pdf

Other links

Publisher's full text

Search in DiVA

By author/editor
Cheregi, OtiliaWagner, RaikFunk, Christiane
By organisation
Department of Chemistry
In the same journal
Frontiers in Plant Science
Chemical SciencesBiochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar
Total: 13 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

Altmetric score

Total: 105 hits
ReferencesLink to record
Permanent link

Direct link