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CO2 limitation induces specific redox-dependent protein phosphorylation in Chlamydomonas reinhardtii
Linköpings universitet, Institutionen för klinisk och experimentell medicin, Cellbiologi. Linköpings universitet, Hälsouniversitetet.
Department of Plant Physiology, Umeå University, Umeå, Sweden.
Linköpings universitet, Institutionen för klinisk och experimentell medicin, Cellbiologi. Linköpings universitet, Hälsouniversitetet.
Linköpings universitet, Institutionen för klinisk och experimentell medicin, Cellbiologi. Linköpings universitet, Hälsouniversitetet.
Vise andre og tillknytning
2006 (engelsk)Inngår i: Proteomics, ISSN 1615-9853, Vol. 6, nr 9, s. 2693-2704Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Acclimation of the green alga Chlamydomonas reinhardtii to limiting environmental CO2 induced specific protein phosphorylation at the surface of photosynthetic thylakoid membranes. Four phosphopeptides were identified and sequenced by nanospray quadrupole TOF MS from the cells acclimating to limiting CO2. One phosphopeptide originated from a protein that has not been annotated. We found that this unknown expressed protein (UEP) was encoded in the genome of C. reinhardtii. Three other phosphorylated peptides belonged to Lci5 protein encoded by the low-CO2-inducible gene 5 (lci5). The phosphorylation sites were mapped in the tandem repeats of Lci5 ensuring phosphorylation of four serine and three threonine residues in the protein. Immunoblotting with Lci5-specific antibodies revealed that Lci5 was localized in chloroplast and confined to the stromal side of the thylakoid membranes. Phosphorylation of Lci5 and UEP occurred strictly at limiting CO2; it required reduction of electron carriers in the thylakoid membrane, but was not induced by light. Both proteins were phosphorylated in the low-CO2-exposed algal mutant deficient in the light-activated protein kinase Stt7. Phosphorylation of previously unknown basic proteins UEP and Lci5 by specific redox-dependent protein kinase(s) in the photosynthetic membranes reveals the early response of green algae to limitation in the environmental inorganic carbon.

sted, utgiver, år, opplag, sider
2006. Vol. 6, nr 9, s. 2693-2704
Emneord [en]
Amino acid sequencing, Chlamydomonas reinhardtii, CO2 limitation, Mass spectrometry, Protein phosphorylation
HSV kategori
Identifikatorer
URN: urn:nbn:se:liu:diva-12927DOI: 10.1002/pmic.200500461OAI: oai:DiVA.org:liu-12927DiVA, id: diva2:17413
Tilgjengelig fra: 2008-02-06 Laget: 2008-02-06 Sist oppdatert: 2009-06-05
Inngår i avhandling
1. Functional proteomics of protein phosphorylation in algal photosynthetic membranes
Åpne denne publikasjonen i ny fane eller vindu >>Functional proteomics of protein phosphorylation in algal photosynthetic membranes
2008 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
Abstract [en]

Plants, green algae and cyanobacteria perform photosynthetic conversion of sunlight into chemical energy in the permanently changing natural environment. For successful survival and growth photosynthetic organisms have developed complex sensing and signaling acclimation mechanisms. The environmentally dependent protein phosphorylation in photosynthetic membranes is implied in the adaptive responses; however, the molecular mechanisms of this regulation are still largely unknown. We used a mass spectrometry-based approach to achieve a comprehensive mapping of the in vivo protein phosphorylation sites within photosynthetic membranes from the green alga Chlamydomonas reinhardtii subjected to distinct environmental conditions known to affect the photosynthetic machinery.

The state transitions process regulating the energy distribution between two photosystems, involves the temporal functional coupling of phosphorylated light-harvesting complexes II (LHCII) to photosystem I (PSI). During state transitions several of the thylakoid proteins undergo redox-controlled phosphorylation-dephosphorylation cycles. This work provided evidences suggesting that redox-dependent phosphorylation-induced structural changes of the minor LHCII antenna protein CP29 determine the affinity of LHCII for either of the two photosystems. In state 1 the doubly phosphorylated CP29 acts as a linker between the photosystem II (PSII) core and the trimeric LHCII whereas in state 2 this quadruply phosphorylated CP29 would migrate to PSI on the PsaH side and provide the docking of LHCII trimers to the PSI complex. Moreover, this study revealed that exposure of Chlamydomonas cells to high light stress caused hyperphosphorylation of CP29 at seven distinct residues and suggested that high light-induced hyperphosphorylation of CP29 may uncouple this protein together with LHCII from both photosystems to minimize the damaging effects of excess light.

Reversible phosphorylation of the PSII reaction center proteins was shown to be essential for the maintenance of active PSII under high light stress. Particularly dephosphorylation of the light-damaged D1 protein, a central functional subunit of the PSII reaction center, is required for its degradation and replacement. We found in the alga the reversible D1 protein phosphorylation, which until our work, has been considered as plant-specific.

We also discovered specific induction of thylakoid protein phosphorylation during adaptation of alga to limiting environmental CO2. One of the phosphorylated proteins has five phosphorylation sites at both serine and treonine residues. The discovered specific low-CO2- and redox-dependent protein phosphorylation may be an early adaptive and signalling response of the green alga to limitation in inorganic carbon.

This work provides the first comprehensive insight into the network of environmentally regulated protein phosphorylation in algal photosynthetic membranes.

sted, utgiver, år, opplag, sider
Linköping University Electronic Press, 2008. s. 40
Serie
Linköping University Medical Dissertations, ISSN 0345-0082 ; 1038
Emneord
Protein phosphorylation, mass spectrometry, photosynthesis, proteomics
HSV kategori
Identifikatorer
urn:nbn:se:liu:diva-10708 (URN)978-91-85523-02-3 (ISBN)
Disputas
2008-02-29, Linden, ingång 65, Hälsouniversitetet, Linköping, 13:00 (engelsk)
Opponent
Veileder
Tilgjengelig fra: 2008-02-06 Laget: 2008-02-06 Sist oppdatert: 2015-11-19

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