Change search
ReferencesLink to record
Permanent link

Direct link
A novel plant protein undergoing light-induced phosphorylation and release from the photosynthetic thylakoid membranes
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Show others and affiliations
2003 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 100, no 2, 757-62 p.Article in journal (Refereed) Published
Abstract [en]

The characteristics of a phosphoprotein with a relative electrophoretic mobility of 12 kDa have been unknown during two decades of studies on redox-dependent protein phosphorylation in plant photosynthetic membranes. Digestion of this protein from spinach thylakoid membranes with trypsin and subsequent tandem nanospray-quadrupole-time-of-flight mass spectrometry of the peptides revealed a protein sequence that did not correspond to any previously known protein. Sequencing of the corresponding cDNA uncovered a gene for a precursor protein with a transit peptide followed by a strongly basic mature protein with a molecular mass of 8,640 Da. Genes encoding homologous proteins were found on chromosome 3 of Arabidopsis and rice as well as in ESTs from 20 different plant species, but not from any other organisms. The protein can be released from the membrane with high salt and is also partially released in response to light-induced phosphorylation of thylakoids, in contrast to all other known thylakoid phosphoproteins, which are integral to the membrane. On the basis of its properties, this plant-specific protein is named thylakoid soluble phosphoprotein of 9 kDa (TSP9). Mass spectrometric analyses revealed the existence of non-, mono-, di-, and triphosphorylated forms of TSP9 and phosphorylation of three distinct threonine residues in the central part of the protein. The phosphorylation and release of TSP9 from the photosynthetic membrane on illumination favor participation of this basic protein in cell signaling and regulation of plant gene expression in response to changing light conditions.

Place, publisher, year, edition, pages
2003. Vol. 100, no 2, 757-62 p.
Keyword [en]
Plant biology
National Category
Natural Sciences
Research subject
Biophysics; Biochemistry
URN: urn:nbn:se:su:diva-33794DOI: 10.1073/pnas.0235452100PubMedID: 12524456OAI: diva2:283599
Available from: 2009-12-29 Created: 2009-12-29 Last updated: 2011-06-14Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Carlberg, Inger
By organisation
Department of Biochemistry and Biophysics
In the same journal
Proceedings of the National Academy of Sciences of the United States of America
Natural Sciences

Search outside of DiVA

GoogleGoogle Scholar
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: 13 hits
ReferencesLink to record
Permanent link

Direct link