Genetic interactions suggest multiple distinct roles of the arch and core helicase domains of Mtr4 in Rrp6 and exosome function

By Klauer A. Alejandra   van Hoof Ambro  

Nucleic Acids Research, Vol. 41, Iss. 1, 2013-01 ,pp. : 533-541

Oxford University Press

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The PMC2NT domain of the catalytic exosome subunit Rrp6p provides the interface for binding with its cofactor Rrp47p, a nucleic acid-binding protein

By Stead Jonathan A.   Costello Joe L.   Livingstone Michaela J.   Mitchell Phil  

Nucleic Acids Research, Vol. 35, Iss. 16, 2007-08 ,pp. : 5556-5567

Oxford University Press

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Deletion of the nuclear exosome component RRP6 leads to continued accumulation of the histone mRNA HTB1 in S-phase of the cell cycle in Saccharomyces cerevisiae

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Nucleic Acids Research, Vol. 35, Iss. 18, 2007-09 ,pp. : 6268-6279

Oxford University Press

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The N-terminal PIN domain of the exosome subunit Rrp44 harbors endonuclease activity and tethers Rrp44 to the yeast core exosome

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Nucleic Acids Research, Vol. 37, Iss. 4, 2009-03 ,pp. : 1127-1140

Oxford University Press

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Temperature-sensitive mutants of the exosome subunit Rrp43p show a deficiency in mRNA degradation and no longer interact with the exosome

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Oxford University Press

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