RNase II structure completes group portrait of 3' exoribonucleases (Q80217869)

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29 December 2019

title

RNase II structure completes group portrait of 3' exoribonucleases (English)

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29 December 2019

author name string

Daneen Grossman

series ordinal

1

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29 December 2019

Ambro van Hoof

series ordinal

2

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29 December 2019

publication date

1 September 2006

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Nature Structural & Molecular Biology

29 December 2019

published in

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29 December 2019

volume

13

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29 December 2019

issue

9

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29 December 2019

page(s)

760-761

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Exoribonucleases and their multiple roles in RNA metabolism

29 December 2019

cites work

1 reference

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Three conserved members of the RNase D family have unique and overlapping functions in the processing of 5S, 5.8S, U4, U5, RNase MRP and RNase P RNAs in yeast

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Ssd1p of Saccharomyces cerevisiae associates with RNA.

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The yeast exosome and human PM-Scl are related complexes of 3' --> 5' exonucleases

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Drosophila gene tazman, an orthologue of the yeast exosome component Rrp44p/Dis3, is differentially expressed during development.

31 March 2020

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

31 March 2020

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The archaeal exosome core is a hexameric ring structure with three catalytic subunits

31 March 2020

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RNA degradation by the exosome is promoted by a nuclear polyadenylation complex

31 March 2020

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Crystal structure of Escherichia coli RNase D, an exoribonuclease involved in structured RNA processing.

31 March 2020

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Structural framework for the mechanism of archaeal exosomes in RNA processing

31 March 2020

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31 March 2020

Identifiers

DOI

10.1038/NSMB0906-760

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16955096%20AND%20SRC:MED&resulttype=core&format=json

29 December 2019

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