SUMO modifications control assembly of synaptonemal complex and polycomplex in meiosis of <i>Saccharomyces cerevisiae</i>

Cheng, Chung-Hsu; Lo, Yu-Hui; Liang, Shu-Shan; Ti, Shih-Chieh; Lin, Feng-Ming; Yeh, Chia-Hui; Huang, Han-Yi; Wang, Ting-Fang

doi:10.1101/gad.1430406

Cited by 255 publications

(426 citation statements)

References 59 publications

Supporting

Mentioning

398

Contrasting

Unclassified

Order By: Relevance

“…Although initial attempts failed to detect activity on a variety of standard substrates (e.g., beta-galactosidase, calf histones, bovine serum albumin, human topoisomerase II), SUMO chains were reproducibly generated in an Slx5-and Slx8-dependent manner. This activity has previously been observed using several SUMO E3 ligases [15,19,43]. As shown in Fig.…”

Section: Slx5 and Slx8 Proteins Stimulate Sumo Conjugation Activity Isupporting

confidence: 78%

“…Mms21 is conserved in humans [17] and co-purifies with the essential Smc5-Smc6 that is required for recombination-mediated DNA repair [16,18]. Zip3 is a meiotic SUMO E3 ligase with an SPRING domain that plays a role in the formation of the synaptonemal complex [19]. In addition to the SP-RING proteins, human cells contain at least two SUMO E3 ligases, RanBP2 and PC2, that lack any form of RING domain [20,21].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Stimulation of in vitro sumoylation by Slx5–Slx8: Evidence for a functional interaction with the SUMO pathway

et al. 2007

View full text Add to dashboard Cite

The yeast genes SLX5 and SLX8 were identified based on their requirement for viability in the absence of the Sgs1 DNA helicase. Loss of these genes results in genome instability, nibbled colonies, and other phenotypes associated with defects in sumoylation. The Slx5 and Slx8 proteins form a stable complex and each subunit contains a single RING-finger domain at its C-terminus. To determine the physiological function of the Slx5-8 complex, we explored its interaction with the SUMO pathway. Curing 2μ circle from the mutants suppressed their nibbled colony phenotype and partially improved their growth rate, but did not affect their sensitivity to hydroxyurea. The increase in sumoylation observed in slx5Δ and slx8Δ mutants was found to be dependent on the Siz1 SUMO ligase. Physical interactions between the Slx5-8 complex and both Ubc9 and Smt3 were identified and characterized. Using in vitro reactions, we show that Slx5, Slx8, or the Slx5-8 complex stimulates the formation of SUMO chains and the sumoylation of a test substrate. Interestingly, a functional RING-finger domain is not required for this stimulation in vitro. These biochemical data demonstrate for the first time that the Slx5-8 complex is capable of interacting directly with the SUMO pathway.

show abstract

Section: Slx5 and Slx8 Proteins Stimulate Sumo Conjugation Activity Isupporting

confidence: 78%

Section: Introductionmentioning

confidence: 99%

Stimulation of in vitro sumoylation by Slx5–Slx8: Evidence for a functional interaction with the SUMO pathway

et al. 2007

View full text Add to dashboard Cite

show abstract

“…12-15 Although the significance of SUMO-2/3 chains remains uncertain, polymeric Smt3 chains may play a functional role during meiotic chromosomal segregation in yeast. 16 Ub/Ubl proteins are synthesized as precursors, and are processed by proteases to their mature form. These enzymes release residues at the Ub/Ubl C-terminus to expose a conserved Cterminal Gly-Gly motif which is then adenylated in an ATP-dependent process by an E1-activating enzyme.…”

Section: Introductionmentioning

confidence: 99%

Structure and Analysis of a Complex between SUMO and Ubc9 Illustrates Features of a Conserved E2-Ubl Interaction

Capili

Lima

2007

Journal of Molecular Biology

128

138

View full text Add to dashboard Cite

SummaryThe SUMO E2 Ubc9 serves as a lynchpin in the SUMO conjugation pathway, interacting with the SUMO E1 during activation, with thioester linked SUMO after E1 transfer and with the substrate and SUMO E3 ligases during conjugation. In this manuscript, we describe the structure determination of a non-covalent complex between human Ubc9 and SUMO-1 at 2.4 Å resolution. Non-covalent interactions between Ubc9 and SUMO are conserved in human and yeast insomuch as human Ubc9 interacts with each of the human SUMO isoforms, and yeast Ubc9 interacts with Smt3, the yeast SUMO ortholog. Structural comparisons reveal similarities to several other non-covalent complexes in the ubiquitin pathway, suggesting that the non-covalent Ubc9-SUMO interface may be important for poly-SUMO chain formation, for E2 recruitment to SUMO conjugated substrates, or for mediating E2 interactions with either E1 or E3 ligases. Biochemical analysis suggests this surface is less important for E1 activation or di-SUMO-2 formation, but more important for E3 interactions and for poly-SUMO chain formation when the chain exceeds more than two SUMO proteins.

show abstract

“…25,26 The functions of sumoylation in higher organisms have been explored in studies on spermatogenesis; it has been shown that sumoylation plays crucial roles in several processes during spermatogenesis, including XY body formation, Figure 1. Subcellular localization of SUMo-1 during mouse oocyte maturation.…”

mentioning

confidence: 99%

The SUMO pathway functions in mouse oocyte maturation

Wang¹,

Ou²,

Tong³

et al. 2010

Cell Cycle

View full text Add to dashboard Cite

SUMO modifications control assembly of synaptonemal complex and polycomplex in meiosis of Saccharomyces cerevisiae

Cited by 255 publications

References 59 publications

Stimulation of in vitro sumoylation by Slx5–Slx8: Evidence for a functional interaction with the SUMO pathway

Stimulation of in vitro sumoylation by Slx5–Slx8: Evidence for a functional interaction with the SUMO pathway

Structure and Analysis of a Complex between SUMO and Ubc9 Illustrates Features of a Conserved E2-Ubl Interaction

The SUMO pathway functions in mouse oocyte maturation

Contact Info

Product

Resources

About