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
Association of small CAB-like proteins (SCPs) of Synechocystis sp. PCC 6803 with Photosystem II
Umeå University, Faculty of Science and Technology, Department of Chemistry. (Arizona State University School of Life Sciences and Center for Bioenergy and Photosynthesis, Tempe, USA)
Umeå University, Faculty of Science and Technology, Department of Chemistry. (Arizona State University School of Life Sciences and Center for Bioenergy and Photosynthesis, Tempe, USA)
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry. (Arizona State University School of Life Sciences and Center for Bioenergy and Photosynthesis, Tempe, USA)
Show others and affiliations
2008 (English)In: Photosynthesis Research, ISSN 0166-8595, E-ISSN 1573-5079, Vol. 95, no 2/3, 135-145 p.Article in journal (Refereed) Published
Abstract [en]

The cyanobacterial small CAB-like proteins (SCPs) are one-helix proteins with compelling similarity to the first and third transmembrane helix of proteins belonging to the CAB family of light-harvesting complex proteins in plants. The SCP proteins are transiently expressed at high light intensity and other stress conditions but their exact function remains largely unknown. Recently we showed association of ScpD with light-stressed, monomeric Photosystem II in Synechocystis sp. PCC 6803 (Yao et al. J Biol Chem 282:267-276, 2007). Here we show that ScpB associates with Photosystem II at normal growth conditions. Moreover, upon introduction of a construct into Synechocystis so that ScpB is expressed continuously under normal growth conditions, ScpE was detected under non-stressed conditions as well, and was copurified with tagged ScpB and Photosystem II. We also report on a one-helix protein, Slr1544, that is somewhat similar to the SCPs and whose gene is cotranscribed with that of ScpD; Slr1544 is another member of the extended light-harvesting-like (Lil) protein family, and we propose to name it LilA.

Place, publisher, year, edition, pages
SpringerLink , 2008. Vol. 95, no 2/3, 135-145 p.
Keyword [en]
Antenna, Chlorophyll-binding protein, Cyanobacteria, Early-light induced proteins (ELIPs), High-light induced proteins (HLIPs), Light-harvesting complex, Synechocystis sp. PCC 6803
Identifiers
URN: urn:nbn:se:umu:diva-16688DOI: 10.1007/s11120-007-9244-3PubMedID: 17912610OAI: oai:DiVA.org:umu-16688DiVA: diva2:156361
Available from: 2008-05-30 Created: 2008-05-30 Last updated: 2017-12-14Bibliographically approved
In thesis
1. The Small Cab-like Proteins in the cyanobacterium Synechocystis sp. PCC 6803
Open this publication in new window or tab >>The Small Cab-like Proteins in the cyanobacterium Synechocystis sp. PCC 6803
2009 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The Small Cab-like Proteins (SCPs) in the cyanobacterium Synechocystis sp. PCC 6803 accumulate in cells grown under different stress conditions. Genes coding for SCPs have been found in all sequenced organisms performing oxygenic photosynthesis and even in the genomes of cyanophages. Deletion of multiple scp genes in Synechocystis resulted in mutants with severely impaired growth and altered pigment content. These findings indicate the importance of SCPs in photosynthesis; however, their specific function is not well understood. SCPs share a chlorophyll-binding motif with the plant light harvesting complex, suggesting that they bind chlorophyll. Here I describe my findings, which unambiguously show that SCPs are able to bind chlorophyll in vitro. Although they affect both the stoichiometric ratio of Photosystem I to II and chlorophyll stability, they do not seem to be directly involved in non-photochemical quenching. I was able to reveal the location of the SCPs within the cyanobacterial cell: in stressed cells they attach to Photosystem II in the thylakoid membrane. Furthermore, I revealed the presence of another light-harvesting like (Lil)/SCP protein in Synechocystis sp. PCC 6803. The gene, slr1544, codifying for this newly characterised LilA protein, co-transcribes together with scpD and also appears to bind to Photosystem II during stress.

Place, publisher, year, edition, pages
Umeå: Umeå universitet, 2009. 49 p.
Keyword
Photosynthesis, Photosystem II, chlorophyll-binding proteins, tetrapyrrole biosynthesis, photodamage, non-photochemical quenching, SCPs, LHCII
National Category
Biochemistry and Molecular Biology Botany
Research subject
Biochemistry
Identifiers
urn:nbn:se:umu:diva-25886 (URN)978-91-7264-849-4 (ISBN)
Distributor:
Kemi, 90187, Umeå
Public defence
2009-10-02, KB3B9, KBChuset, Umeå Universitet, Umeå, 13:00 (English)
Opponent
Supervisors
Available from: 2009-09-11 Created: 2009-09-09 Last updated: 2009-09-11Bibliographically approved
2. Stress response in the cyanobacterium Synechocystis sp. PCC 6803
Open this publication in new window or tab >>Stress response in the cyanobacterium Synechocystis sp. PCC 6803
2011 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Adaptation to environmental changes is important for the survival of living organisms. Under extreme abiotic conditions, organic molecules (such as lipids, proteins and nucleic acids) are prone to damage. Under these conditions stress response mechanisms are activated, either to prevent the source of damage or to promote the rapid turnover of damaged molecules. Like all photoautotrophic organisms, cyanobacteria are sensitive to high light intensity and oxidative stress, which induces damage to the photosynthetic apparatus. My thesis is divided in two subjects related to particular stress responses in the cyanobacterium Synechocystis sp. PCC 6803: 1) the role of Deg/HtrA proteases and 2) investigations on the small CAB-like proteins.

Deg/HtrA proteases are ATP-independent serine endopeptidases with a characteristic C-terminal PDZ domain. These proteases are largely dispersed among living organisms, with many different functions, mostly involved in protein quality control. The genome of Synechocystis sp. PCC 6803 contains three genes coding for Deg/HtrA proteases: HtrA, HhoA and HhoB. These proteases are essential for survival under high light and heat stress, and may overlap in their functions. During my Ph.D. studies I focused on the identification of the precise localization of the Deg/HtrA proteases in the cyanobacterial cell, analyzed the biochemical properties of recombinant Synechocystis Deg/HtrA proteases in vitro and adopted proteomic and metabolomic approaches to study the physiological importance of these proteases. My data show that Deg/HtrA proteases are not only important in stress response mechanisms under adverse conditions, but are also involved in the stabilization of important physiological processes, such as polysaccharides biosynthesis and peptidoglycan turnover.

The small CAB-like proteins (SCPs) belong to the light harvesting-like family of stress induced proteins and are thought to be involved in the photoprotection of the photosynthetic apparatus. Five small CAB-like proteins where identified in Synechocystis sp. PCC 6803 (ScpA-E). In my studies I identified another relative to the SCPs, LilA, which I found to be co-transcribed with ScpD. I also focused on the subcellular localization and identification of potential interaction partners of the SCPs.

Place, publisher, year, edition, pages
Umeå: Department of Chemistry, Umeå University, 2011. 49 p.
Keyword
Cyanobacteria, High light, heat stress, ROS, Photosynthesis, Photosystem II, Deg/HtrA proteases, small CAB-like proteins, Refraction-2D™, MALDI-TOF, 2D-gel, GC-MS, PCA, OPLS-DA, EPS, S-layer
National Category
Biochemistry and Molecular Biology
Research subject
Biochemistry
Identifiers
urn:nbn:se:umu:diva-43086 (URN)978-91-7459-201-6 (ISBN)
Public defence
2011-05-13, KBC-huset, KB3B1, Umeå University, Umeå, Sweden, 13:00 (English)
Opponent
Supervisors
Available from: 2011-04-20 Created: 2011-04-18 Last updated: 2011-04-19Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Hernández-Prieto, Miguel AngelKieselbach, ThomasMiranda, HélderFunk, Christiane
By organisation
Department of Chemistry
In the same journal
Photosynthesis Research

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 140 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