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The SUMO (Small Ubiquitin‐like Modifier) system in Chlamydomonas reinhardtii
Author(s) -
Bailey Cheryl,
Wang Ying,
Weeks Donald
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a270-c
Subject(s) - chlamydomonas reinhardtii , sumo protein , ubiquitin , biology , arabidopsis , homology (biology) , sumo enzymes , chlamydomonas , microbiology and biotechnology , gene , genetics , mutant
SUMO ( S mall u biquitin‐like mo difier), is a member of the family of ubiquitin‐like polypeptides that become covalentlyattached to intracellular target proteins. SUMOylation can alter the function, location, and/or half‐life of target proteins. Here we describe identification of SUMOylation proteins in Chlamydomonas reinhardtii . Through analysis of the Chlamydomonas reinhardtii genome and sequence similarity to SUMOylation proteins in other organisms, three potential SUMO proteins have been identified in C. reinhardtii : SUMO94, SUMO132 and SUMO89. SUMO94 shows homology to human SUMO‐1, while SUMO132 and SUMO89 show homology to human SUMO‐2, respectively. Northern analysis shows robust expression of SUMO94C in both high and low CO2 growth conditions, with lower expression levels of SUMO132 and SUMO89 in both high and low CO 2 conditions. Antibodies against Arabidopsis thaliana SUMO1 and C. reinhardtii SUMO94 detected a variety of SUMOylated modified proteins in C. reinhardtii in various stress conditions. These findings allow further elucidation of the both proteins targeted for SUMOylation and the SUMOylation mechanism in C. reinhardtii .