title: NMR assignments of ubiquitin fold domain (UFD) in SUMO-activating enzyme subunit 2 from rice.
abstract: The small ubiquitin-related modifier (SUMO) is a ubiquitin-like post-translational modifier that alters the localization, activity, or stability of many proteins. In the sumoylation process, an activated SUMO is transferred from SUMO-activating enzyme E1 complex (SAE1/SAE2) to SUMO-conjugating enzyme E2 (Ubc9). Among the multiple domains in E1, a C-terminal ubiquitin fold domain (UFD) of SAE2 shows high affinity for Ubc9, implying that UFD will be functionally important. We report NMR chemical shift assignments of UFD in SAE2 from rice. Almost all the resonances of UFD were assigned uniquely, representing a single conformation of UFD in solution. This is a contrast to the previous report for the corresponding UFD of human SAE2 which shows two conformational states. The secondary structure prediction of UFD in rice SAE2 shows the similar overall structure to the crystal structures of UFD in other E1 proteins such as SAE2 of human and yeast, ubiquitin-activating enzyme of yeast, and NEDD8-activating enzyme E1 catalytic subunit of human. Concomitantly, differences in the length of helices, strands, and loops are observed, particularly in the binding region to E2, supposing the variation in the UFD-E2 binding mode which may play a critical role in determining E1-E2 specificity.
authors.affiliation: Protein Research Unit, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki, 305-8602, Japan.
authors.forename: Rintaro
authors.initials: R
authors.lastname: Suzuki
authors.forename: Wataru
authors.initials: W
authors.lastname: Tsuchiya
authors.forename: Heisaburo
authors.initials: H
authors.lastname: Shindo
authors.forename: Toshimasa
authors.initials: T
authors.lastname: Yamazaki
mesh_terms: D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D012275:Oryza / Q000737:chemistry / Q000201:enzymology*; D010940:Plant Proteins / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry; D016415:Sequence Alignment; D044764:Ubiquitin-Activating Enzymes / Q000737:chemistry*
chemical_list: D010940:Plant Proteins; D021122:Protein Subunits; D011994:Recombinant Proteins; D044764:Ubiquitin-Activating Enzymes