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

ABSTRACT: 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 ?-strand (?3) and ?3-?2 loop, instead of the canonical ?4 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 ?3-?2 loop is relatively rigid although it might have intrinsic dynamic profile. The positively charged residues of the ?3-?2 loop are involved in interacting with the C-terminal leucine-rich repeat-like domain of Rpn1.

SUBMITTER: Yun JH 

PROVIDER: S-EPMC3646893 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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

Yun Ji-Hye JH   Ko Sunggeon S   Lee Chung-Kyung CK   Cheong Hae-Kap HK   Cheong Chaejoon C   Yoon Jong-Bok JB   Lee Weontae W  

PloS one 20130507 5

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, i  ...[more]

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