Solution structure and Rpn1 interaction of the UBL domain of human RNA polymerase II C-terminal domain phosphatase

• Published in: PloS one Vol. 8; no. 5; p. e62981
• Main Authors: Yun, Ji-Hye, Ko, Sunggeon, Lee, Chung-Kyung, Cheong, Hae-Kap, Cheong, Chaejoon, Yoon, Jong-Bok, Lee, Weontae
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 07-05-2013; Public Library of Science (PLoS)
• Subjects: Amino Acid Motifs; Amino Acid Sequence; Automation; Biochemistry; Biology; Biotechnology; DNA-directed RNA polymerase; Experiments; Humans; Leucine; Life sciences; Magnetic resonance; Magnetic resonance spectroscopy; Models, Molecular; Molecular Sequence Data; NMR; Nuclear magnetic resonance; Nuclear magnetic resonance spectroscopy; Nuclear Proteins - chemistry; Nuclear Proteins - metabolism; Phosphatase; Phosphatases; Phosphoprotein Phosphatases - chemistry; Phosphoprotein Phosphatases - metabolism; Proteasomes; Protein Structure, Tertiary; Proteins; Regulation; Ribonucleic acid; RNA; RNA polymerase; RNA polymerase II; Solutions; Spectroscopy; Spectrum analysis; TNF Receptor-Associated Factor 2; Topology; Tumor Necrosis Factor Receptor-Associated Peptides and Proteins - metabolism; Ubiquitin; United States > US
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0062981

The ubiquitin-like modifier (UBL) domain of ubiquitin-like domain proteins (UDPs) interacts specifically with subunits of the 26 S proteasome. A novel UDP, ubiquitin-like domain-containing C-terminal domain phosphatase (UBLCP1), has been identified as an interacting partner of the 26 S proteasome. We determined the high-resolution solution structure of the UBL domain of human UBLCP1 by nuclear magnetic resonance spectroscopy. The UBL domain of hUBLCP1 has a unique β-strand (β3) and β3-α2 loop, instead of the canonical β4 observed in other UBL domains. The molecular topology and secondary structures are different from those of known UBL domains including that of fly UBLCP1. Data from backbone dynamics shows that the β3-α2 loop is relatively rigid although it might have intrinsic dynamic profile. The positively charged residues of the β3-α2 loop are involved in interacting with the C-terminal leucine-rich repeat-like domain of Rpn1.