| Structural highlights
Function
[SUMO_CAEEL] Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process (PubMed:11806825). Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction (PubMed:11806825, PubMed:25475837). Covalent attachment to its substrates requires prior activation by the E1 complex aos-1-uba-2 and linkage to the E2 enzyme ubc-9, and can be promoted by an E3 ligase such as gei-17 (PubMed:15107848, PubMed:16701625). Required for embryonic development, fertility, vulval morphogenesis and inhibition of vulval cell fates (PubMed:15466489, PubMed:15689373, PubMed:15990876, PubMed:24349540). Probably by sumoylating bet-1, prevents muscle myosin depletion in aging adults probably by preventing myoblast growth factor receptor egl-15 overexpression (PubMed:24285704). Plays a role in the attenuation of the let-60/ras pathway (PubMed:24349540, PubMed:24285704).[1] [2] [3] [4] [5] [6] [7] [8]
Publication Abstract from PubMed
SUMO proteins are important post-translational modifiers involved in multiple cellular pathways in eukaryotes, especially during the different developmental stages in multicellular organisms. The nematode C. elegans is a well known model system for studying metazoan development and has a single SUMO homolog, SMO-1. Interestingly, SMO-1 modification is linked to embryogenesis and development in the nematode. However, high-resolution information about SMO-1 and the mechanism of its conjugation is lacking. In this work, we report the high-resolution three dimensional structure of SMO-1 solved by NMR spectroscopy. SMO-1 has flexible N-terminal and C-terminal tails on either side of a rigid beta-grasp folded core. While the sequence of SMO-1 is more similar to SUMO1, the electrostatic surface features of SMO-1 resemble more with SUMO2/3. SMO-1 can bind to typical SUMO Interacting Motifs (SIMs). SMO-1 can also conjugate to a typical SUMOylation consensus site as well as to its natural substrate HMR-1. Poly-SMO-1 chains were observed in-vitro even though SMO-1 lacks any consensus SUMOylation site. Typical deSUMOylation enzymes like Senp2 can cleave the poly-SMO-1 chains. Despite being a single gene, the SMO-1 structure allows it to function in a large repertoire of signaling pathways involving SUMO in C. elegans. Structural and functional features of SMO-1 studies described here will be useful to understand its role in development.
Structural and functional analysis of SMO-1, the SUMO homolog in Caenorhabditis elegans.,Surana P, Gowda CM, Tripathi V, Broday L, Das R PLoS One. 2017 Oct 18;12(10):e0186622. doi: 10.1371/journal.pone.0186622., eCollection 2017. PMID:29045470[9]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jones D, Crowe E, Stevens TA, Candido EP. Functional and phylogenetic analysis of the ubiquitylation system in Caenorhabditis elegans: ubiquitin-conjugating enzymes, ubiquitin-activating enzymes, and ubiquitin-like proteins. Genome Biol. 2002;3(1):RESEARCH0002. Epub 2001 Dec 12. PMID:11806825
- ↑ Zhang H, Smolen GA, Palmer R, Christoforou A, van den Heuvel S, Haber DA. SUMO modification is required for in vivo Hox gene regulation by the Caenorhabditis elegans Polycomb group protein SOP-2. Nat Genet. 2004 May;36(5):507-11. Epub 2004 Apr 11. PMID:15107848 doi:https://dx.doi.org/10.1038/ng1336
- ↑ Broday L, Kolotuev I, Didier C, Bhoumik A, Gupta BP, Sternberg PW, Podbilewicz B, Ronai Z. The small ubiquitin-like modifier (SUMO) is required for gonadal and uterine-vulval morphogenesis in Caenorhabditis elegans. Genes Dev. 2004 Oct 1;18(19):2380-91. PMID:15466489 doi:https://dx.doi.org/10.1101/gad.1227104
- ↑ Leight ER, Glossip D, Kornfeld K. Sumoylation of LIN-1 promotes transcriptional repression and inhibition of vulval cell fates. Development. 2005 Mar;132(5):1047-56. Epub 2005 Feb 2. PMID:15689373 doi:https://dx.doi.org/10.1242/dev.01664
- ↑ Poulin G, Dong Y, Fraser AG, Hopper NA, Ahringer J. Chromatin regulation and sumoylation in the inhibition of Ras-induced vulval development in Caenorhabditis elegans. EMBO J. 2005 Jul 20;24(14):2613-23. Epub 2005 Jun 30. PMID:15990876 doi:https://dx.doi.org/10.1038/sj.emboj.7600726
- ↑ Roy Chowdhuri S, Crum T, Woollard A, Aslam S, Okkema PG. The T-box factor TBX-2 and the SUMO conjugating enzyme UBC-9 are required for ABa-derived pharyngeal muscle in C. elegans. Dev Biol. 2006 Jul 15;295(2):664-77. Epub 2006 Apr 7. PMID:16701625 doi:https://dx.doi.org/10.1016/j.ydbio.2006.04.001
- ↑ Fisher K, Gee F, Wang S, Xue F, Knapp S, Philpott M, Wells C, Rodriguez M, Snoek LB, Kammenga J, Poulin GB. Maintenance of muscle myosin levels in adult C. elegans requires both the double bromodomain protein BET-1 and sumoylation. Biol Open. 2013 Dec 15;2(12):1354-63. doi: 10.1242/bio.20136007. PMID:24285704 doi:https://dx.doi.org/10.1242/bio.20136007
- ↑ Gee F, Fisher K, Klemstein U, Poulin GB. An RNAi-based dimorphic genetic screen identified the double bromodomain protein BET-1 as a sumo-dependent attenuator of RAS-mediated signalling. PLoS One. 2013 Dec 10;8(12):e83659. doi: 10.1371/journal.pone.0083659., eCollection 2013. PMID:24349540 doi:https://dx.doi.org/10.1371/journal.pone.0083659
- ↑ Surana P, Gowda CM, Tripathi V, Broday L, Das R. Structural and functional analysis of SMO-1, the SUMO homolog in Caenorhabditis elegans. PLoS One. 2017 Oct 18;12(10):e0186622. doi: 10.1371/journal.pone.0186622., eCollection 2017. PMID:29045470 doi:https://dx.doi.org/10.1371/journal.pone.0186622
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