14-3-3 proteins are constituents of the insoluble glycoprotein framework of the chlamydomonas cell wall.
dc.contributor.author | Voigt, Jürgen | |
dc.contributor.author | Frank, Ronald | |
dc.date.accessioned | 2017-02-01T10:45:59Z | |
dc.date.available | 2017-02-01T10:45:59Z | |
dc.date.issued | 2003-06 | |
dc.identifier.citation | 14-3-3 proteins are constituents of the insoluble glycoprotein framework of the chlamydomonas cell wall. 2003, 15 (6):1399-413 Plant Cell | en |
dc.identifier.issn | 1040-4651 | |
dc.identifier.pmid | 12782732 | |
dc.identifier.uri | http://hdl.handle.net/10033/620800 | |
dc.description.abstract | The cell wall of the unicellular green alga Chlamydomonas reinhardtii consists predominantly of Hyp-rich glycoproteins, which also occur in the extracellular matrix of multicellular green algae and higher plants. In addition to the Hyp-rich polypeptides, the insoluble glycoprotein framework of the Chlamydomonas cell wall contains minor amounts of 14-3-3 proteins, as revealed by immunochemical studies and mass spectroscopic analysis of tryptic peptides. Polypeptides immunologically related to the 14-3-3 proteins also were found in the culture medium of Chlamydomonas. The levels of two of these 14-3-3-related polypeptides were decreased in the culture medium of the wall-deficient mutant cw-15. These findings indicate that 14-3-3 proteins are involved in the cross-linking of Hyp-rich glycoproteins in the Chlamydomonas cell wall. | |
dc.language.iso | en | en |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/4.0/ | * |
dc.subject.mesh | 14-3-3 Proteins | en |
dc.subject.mesh | Algal Proteins | en |
dc.subject.mesh | Amino Acid Sequence | en |
dc.subject.mesh | Animals | en |
dc.subject.mesh | Cell Wall | en |
dc.subject.mesh | Chlamydomonas reinhardtii | en |
dc.subject.mesh | Electrophoresis, Polyacrylamide Gel | en |
dc.subject.mesh | Epitope Mapping | en |
dc.subject.mesh | Glycoproteins | en |
dc.subject.mesh | Glycosylation | en |
dc.subject.mesh | Immunoblotting | en |
dc.subject.mesh | Molecular Sequence Data | en |
dc.subject.mesh | Protein Isoforms | en |
dc.subject.mesh | Sequence Analysis, Protein | en |
dc.subject.mesh | Tyrosine 3-Monooxygenase | en |
dc.title | 14-3-3 proteins are constituents of the insoluble glycoprotein framework of the chlamydomonas cell wall. | en |
dc.type | Article | en |
dc.contributor.department | Helmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany. | en |
dc.identifier.journal | The Plant cell | en |
refterms.dateFOA | 2018-06-12T17:53:43Z | |
html.description.abstract | The cell wall of the unicellular green alga Chlamydomonas reinhardtii consists predominantly of Hyp-rich glycoproteins, which also occur in the extracellular matrix of multicellular green algae and higher plants. In addition to the Hyp-rich polypeptides, the insoluble glycoprotein framework of the Chlamydomonas cell wall contains minor amounts of 14-3-3 proteins, as revealed by immunochemical studies and mass spectroscopic analysis of tryptic peptides. Polypeptides immunologically related to the 14-3-3 proteins also were found in the culture medium of Chlamydomonas. The levels of two of these 14-3-3-related polypeptides were decreased in the culture medium of the wall-deficient mutant cw-15. These findings indicate that 14-3-3 proteins are involved in the cross-linking of Hyp-rich glycoproteins in the Chlamydomonas cell wall. |