Revised annotation and extended characterizations of components of the Chlamydomonas reinhardtii SUMOylation system
Abstract Small ubiquitin‐like modifier (SUMO) conjugation, or SUMOylation, is a reversible post‐translational modification that is important for regulation of many cellular processes including cell division cycle in the eukaryotic kingdom. However, only a portion of the components of the Chlamydomon...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2020-09-01
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| Series: | Plant Direct |
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| Online Access: | https://doi.org/10.1002/pld3.266 |
| _version_ | 1819296726269296640 |
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| author | Yen‐Ling Lin Chin‐Lin Chung Pin‐jui Huang Chun‐Han Chen Su‐Chiung Fang |
| author_facet | Yen‐Ling Lin Chin‐Lin Chung Pin‐jui Huang Chun‐Han Chen Su‐Chiung Fang |
| author_sort | Yen‐Ling Lin |
| collection | DOAJ |
| description | Abstract Small ubiquitin‐like modifier (SUMO) conjugation, or SUMOylation, is a reversible post‐translational modification that is important for regulation of many cellular processes including cell division cycle in the eukaryotic kingdom. However, only a portion of the components of the Chlamydomonas SUMOylation system are known and their functions and regulation investigated. The present studies are aimed at extending discovery and characterization of new components and improving the annotation and nomenclature of all known proteins and genes involved in the system. Even though only one copy of the heterodimerized SUMO‐activating enzyme, SAE1 and SAE2, was identified, the number of SUMO‐conjugating enzymes (SCEs) and SUMO proteases/isopeptidase was expanded in Chlamydomonas. Using the reconstituted SUMOylation system, we showed that SCE1, SCE2, and SCE3 have SUMO‐conjugating activity. In addition to SUMOylation, components required for other post‐translational modifications such as NEDDylation, URMylation, and UFMylation, were confirmed to be present in Chlamydomonas. Our data also showed that besides isopeptidase activity, the SUMO protease domain of SUPPRESSOR OF MAT3 7/SENTRIN‐SPECIFIC PROTEASE 1 (SMT7/SENP1) has endopeptidase activity that is capable of processing SUMO precursors. Moreover, the key cell cycle regulators of Chlamydomonas E2F1, DP1, CDKG1, CYCD2, and CYCD3 were SUMOylated in vitro, suggesting SUMOylation may be part of regulatory pathway modulating cell cycle regulators. |
| first_indexed | 2024-12-24T05:02:41Z |
| format | Article |
| id | doaj.art-c7606b2b166748ec976b277132213e96 |
| institution | Directory Open Access Journal |
| issn | 2475-4455 |
| language | English |
| last_indexed | 2024-12-24T05:02:41Z |
| publishDate | 2020-09-01 |
| publisher | Wiley |
| record_format | Article |
| series | Plant Direct |
| spelling | doaj.art-c7606b2b166748ec976b277132213e962022-12-21T17:13:56ZengWileyPlant Direct2475-44552020-09-0149n/an/a10.1002/pld3.266Revised annotation and extended characterizations of components of the Chlamydomonas reinhardtii SUMOylation systemYen‐Ling Lin0Chin‐Lin Chung1Pin‐jui Huang2Chun‐Han Chen3Su‐Chiung Fang4Biotechnology Center in Southern Taiwan Academia Sinica Tainan TaiwanBiotechnology Center in Southern Taiwan Academia Sinica Tainan TaiwanBiotechnology Center in Southern Taiwan Academia Sinica Tainan TaiwanBiotechnology Center in Southern Taiwan Academia Sinica Tainan TaiwanBiotechnology Center in Southern Taiwan Academia Sinica Tainan TaiwanAbstract Small ubiquitin‐like modifier (SUMO) conjugation, or SUMOylation, is a reversible post‐translational modification that is important for regulation of many cellular processes including cell division cycle in the eukaryotic kingdom. However, only a portion of the components of the Chlamydomonas SUMOylation system are known and their functions and regulation investigated. The present studies are aimed at extending discovery and characterization of new components and improving the annotation and nomenclature of all known proteins and genes involved in the system. Even though only one copy of the heterodimerized SUMO‐activating enzyme, SAE1 and SAE2, was identified, the number of SUMO‐conjugating enzymes (SCEs) and SUMO proteases/isopeptidase was expanded in Chlamydomonas. Using the reconstituted SUMOylation system, we showed that SCE1, SCE2, and SCE3 have SUMO‐conjugating activity. In addition to SUMOylation, components required for other post‐translational modifications such as NEDDylation, URMylation, and UFMylation, were confirmed to be present in Chlamydomonas. Our data also showed that besides isopeptidase activity, the SUMO protease domain of SUPPRESSOR OF MAT3 7/SENTRIN‐SPECIFIC PROTEASE 1 (SMT7/SENP1) has endopeptidase activity that is capable of processing SUMO precursors. Moreover, the key cell cycle regulators of Chlamydomonas E2F1, DP1, CDKG1, CYCD2, and CYCD3 were SUMOylated in vitro, suggesting SUMOylation may be part of regulatory pathway modulating cell cycle regulators.https://doi.org/10.1002/pld3.266cell cycleChlamydomonas reinhardtiideSUMOylationSUMOylation |
| spellingShingle | Yen‐Ling Lin Chin‐Lin Chung Pin‐jui Huang Chun‐Han Chen Su‐Chiung Fang Revised annotation and extended characterizations of components of the Chlamydomonas reinhardtii SUMOylation system Plant Direct cell cycle Chlamydomonas reinhardtii deSUMOylation SUMOylation |
| title | Revised annotation and extended characterizations of components of the Chlamydomonas reinhardtii SUMOylation system |
| title_full | Revised annotation and extended characterizations of components of the Chlamydomonas reinhardtii SUMOylation system |
| title_fullStr | Revised annotation and extended characterizations of components of the Chlamydomonas reinhardtii SUMOylation system |
| title_full_unstemmed | Revised annotation and extended characterizations of components of the Chlamydomonas reinhardtii SUMOylation system |
| title_short | Revised annotation and extended characterizations of components of the Chlamydomonas reinhardtii SUMOylation system |
| title_sort | revised annotation and extended characterizations of components of the chlamydomonas reinhardtii sumoylation system |
| topic | cell cycle Chlamydomonas reinhardtii deSUMOylation SUMOylation |
| url | https://doi.org/10.1002/pld3.266 |
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