Functional proteomics of circadian expressed proteins from Chlamydomonas reinhardtii.

Abstract:

:In this study, functional proteomics was successfully applied for the characterization of circadian expressed, basic proteins. For this purpose, we have chosen the green model alga Chlamydomonas reinhardtii since its entire nuclear genome is available and it is ideally suited for biochemical enrichment procedures. Proteins from cells harvested during subjective day and night were heparin affinity purified. They were separated by two-dimensional gel electrophoresis suited for basic proteins and analyzed after tryptic digestion by electrospray ionization mass spectrometry. We can show for the first time that the expressions of a protein disulfide isomerase-like protein and a tetratricopeptide repeat protein change in a circadian manner. Interestingly, both proteins are known to be interaction partners in multiprotein complexes including RNA binding proteins.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Wagner V,Fiedler M,Markert C,Hippler M,Mittag M

doi

10.1016/S0014-5793(04)00051-1

keywords:

subject

Has Abstract

pub_date

2004-02-13 00:00:00

pages

129-35

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579304000511

journal_volume

559

pub_type

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