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Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain.

ABSTRACT: The multisubunit eukaryotic exosome is an essential RNA processing and degradation machine. In its nuclear form, the exosome associates with the auxiliary factor Rrp6p, which participates in both RNA processing and degradation reactions. The crystal structure of Saccharomyces cerevisiae Rrp6p displays a conserved RNase D core with a flanking HRDC (helicase and RNase D C-terminal) domain in an unusual conformation shown to be important for the processing function of the enzyme. Complexes with AMP and UMP, the products of the RNA degradation process, reveal how the protein specifically recognizes ribonucleotides and their bases. Finally, in vivo mutational studies show the importance of the domain contacts for the processing function of Rrp6p and highlight fundamental differences between the protein and its prokaryotic RNase D counterparts.

SUBMITTER: Midtgaard SF 

PROVIDER: S-EPMC2131688 | biostudies-literature | 2006 Aug

REPOSITORIES: biostudies-literature

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Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain.

Midtgaard Søren F SF   Assenholt Jannie J   Jonstrup Anette Thyssen AT   Van Lan B LB   Jensen Torben Heick TH   Brodersen Ditlev E DE  

Proceedings of the National Academy of Sciences of the United States of America 20060801 32

The multisubunit eukaryotic exosome is an essential RNA processing and degradation machine. In its nuclear form, the exosome associates with the auxiliary factor Rrp6p, which participates in both RNA processing and degradation reactions. The crystal structure of Saccharomyces cerevisiae Rrp6p displays a conserved RNase D core with a flanking HRDC (helicase and RNase D C-terminal) domain in an unusual conformation shown to be important for the processing function of the enzyme. Complexes with AMP  ...[more]

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