Abstract
SUMO-binding proteins interact with SUMO modified proteins to mediate a wide range of functional consequences. Here, we report the identification of a new SUMO-binding protein, ZNF261. Four human proteins including ZNF261, ZNF198, ZNF262, and ZNF258 contain a stretch of tandem zinc fingers called myeloproliferative and mental retardation (MYM)-type zinc fingers. We demonstrated that MYM-type zinc fingers from ZNF261 and ZNF198 are necessary and sufficient for SUMO-binding and that individual MYM-type zinc fingers function as SUMO-interacting motifs (SIMs). Our binding studies revealed that the MYM-type zinc fingers from ZNF261 and ZNF198 interact with the same surface on SUMO-2 recognized by the archetypal consensus SIM. We also present evidence that MYM-type zinc fingers in ZNF261 contain zinc, but that zinc is not required for SUMO-binding. Immunofluorescence microscopy studies using truncated fragments of ZNF198 revealed that MYM-type zinc fingers of ZNF198 are necessary for localization to PML-nuclear bodies (PML-NBs). In summary, our studies have identified and characterized the SUMO-binding activity of the MYM-type zinc fingers in ZNF261 and ZNF198.
Highlights
Small Ubiquitin-related Modifiers (SUMOs) are reversible posttranslational protein modifications that are conjugated to lysine residues on substrate proteins by an enzymatic cascade
Microarrays were probed with fluorescently labeled SUMO-1, SUMO-2, and a linear polymeric SUMO-2 referred to as SUMO-2(x3) that consists of three consecutive SUMO-2 proteins
myeloproliferative and mental retardation (MYM)-Type Zinc Fingers and classical SUMO-interacting motifs (SIMs) interact with a common surface on SUMO-2
Summary
Small Ubiquitin-related Modifiers (SUMOs) are reversible posttranslational protein modifications that are conjugated to lysine residues on substrate proteins by an enzymatic cascade. Interactions between SUMO-modified proteins and SUMO-binding proteins containing SUMO-interacting motifs (SIMs) regulate a wide range of functional consequences including formation of multi-protein complexes and changes in protein localization, activity, solubility, and stability [1,2]. The functional diversity of the SUMO signal is due, in part, to expression of three SUMO paralogs and formation of polymeric SUMO. Mammals contain three isoforms of SUMO known as SUMO-1, SUMO-2 and SUMO-3. SUMO-1 is ,50% identical to SUMO-2 and SUMO3. SUMO-2 and SUMO-3 are frequently referred to as SUMO-2/ 3 because they are ,96% identical and may be functionally redundant. SUMO-2/3 contains a consensus SUMOylation motif, YKXE/D, and can readily form polymeric chains
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