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

Søren Fuglsang Midtgaard; Jannie Assenholt; Anette Thyssen Jonstrup; Lan Bich Van; Torben Heick Jensen; Ditlev Egeskov Brodersen

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

Søren Fuglsang Midtgaard, Jannie Assenholt, Anette Thyssen Jonstrup, Lan Bich Van, Torben Heick Jensen, Ditlev Egeskov Brodersen

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

73 Citationer (Scopus)

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.

Originalsprog	Engelsk
Tidsskrift	Proceedings of the National Academy of Sciences (PNAS)
Vol/bind	103
Nummer	32
Sider (fra-til)	11898-11903
ISSN	0027-8424
Status	Udgivet - 2006

Citationsformater

@article{c085aff0a6e511dbbee902004c4f4f50,

title = "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.",

author = "Midtgaard, {S{\o}ren Fuglsang} and Jannie Assenholt and Jonstrup, {Anette Thyssen} and Van, {Lan Bich} and Jensen, {Torben Heick} and Brodersen, {Ditlev Egeskov}",

year = "2006",

language = "English",

volume = "103",

pages = "11898--11903",

journal = "Proceedings of the National Academy of Sciences (PNAS)",

issn = "0027-8424",

publisher = "National Academy of Sciences",

number = "32",

}

Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain. / Midtgaard, Søren Fuglsang; Assenholt, Jannie; Jonstrup, Anette Thyssen et al.
I: Proceedings of the National Academy of Sciences (PNAS), Bind 103, Nr. 32, 2006, s. 11898-11903.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

TY - JOUR

T1 - Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain

AU - Midtgaard, Søren Fuglsang

AU - Assenholt, Jannie

AU - Jonstrup, Anette Thyssen

AU - Van, Lan Bich

AU - Jensen, Torben Heick

AU - Brodersen, Ditlev Egeskov

PY - 2006

Y1 - 2006

N2 - 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.

AB - 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.

M3 - Journal article

SN - 0027-8424

VL - 103

SP - 11898

EP - 11903

JO - Proceedings of the National Academy of Sciences (PNAS)

JF - Proceedings of the National Academy of Sciences (PNAS)

IS - 32

ER -

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

Abstract

Fingeraftryk

Citationsformater