The RNA polymerase 2 C-terminal domain-interacting domain of yeast Nrd1 contributes to the choice of termination pathway and couples to RNA processing by the nuclear exosome

Dong Hyuk Heo; Inhea Yoo; Jiwon Kong; Michael Lidschreiber; Andreas Mayer; Byung Yi Choi; Yoonsoo Hahn; Patrick Cramer; Stephen Buratowski; Minkyu Kim

doi:10.1074/jbc.M113.508267

The RNA polymerase 2 C-terminal domain-interacting domain of yeast Nrd1 contributes to the choice of termination pathway and couples to RNA processing by the nuclear exosome

Dong Hyuk Heo, Inhea Yoo, Jiwon Kong, Michael Lidschreiber, Andreas Mayer, Byung Yi Choi, Yoonsoo Hahn, Patrick Cramer, Stephen Buratowski, Minkyu Kim

Research output: Contribution to journal › Article › peer-review

24 Scopus citations

Abstract

Background: Distinct termination pathways for yeast RNA polymerase II (RNApII) employ proteins (Nrd1 and Rtt103) recognizing different phospho-forms of the RNApII C-terminal domain (CTD). Results: Alteration of CTD-binding specificity of Nrd1 significantly affects RNApII termination. Conclusion: Differential interaction between RNApII CTD and termination factors is crucial in choosing a termination pathway. Significance: CTD-interacting domain of Nrd1 couples termination and RNA processing by the nuclear exosome.

Original language	English (US)
Pages (from-to)	36676-36690
Number of pages	15
Journal	Journal of Biological Chemistry
Volume	288
Issue number	51
DOIs	https://doi.org/10.1074/jbc.M113.508267
State	Published - Dec 20 2013
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1074/jbc.M113.508267

Cite this

Heo, D. H., Yoo, I., Kong, J., Lidschreiber, M., Mayer, A., Choi, B. Y., Hahn, Y., Cramer, P., Buratowski, S., & Kim, M. (2013). The RNA polymerase 2 C-terminal domain-interacting domain of yeast Nrd1 contributes to the choice of termination pathway and couples to RNA processing by the nuclear exosome. Journal of Biological Chemistry, 288(51), 36676-36690. https://doi.org/10.1074/jbc.M113.508267

The RNA polymerase 2 C-terminal domain-interacting domain of yeast Nrd1 contributes to the choice of termination pathway and couples to RNA processing by the nuclear exosome. / Heo, Dong Hyuk; Yoo, Inhea; Kong, Jiwon et al.
In: Journal of Biological Chemistry, Vol. 288, No. 51, 20.12.2013, p. 36676-36690.

Research output: Contribution to journal › Article › peer-review

Heo, DH, Yoo, I, Kong, J, Lidschreiber, M, Mayer, A, Choi, BY, Hahn, Y, Cramer, P, Buratowski, S & Kim, M 2013, 'The RNA polymerase 2 C-terminal domain-interacting domain of yeast Nrd1 contributes to the choice of termination pathway and couples to RNA processing by the nuclear exosome', Journal of Biological Chemistry, vol. 288, no. 51, pp. 36676-36690. https://doi.org/10.1074/jbc.M113.508267

@article{994cf5866cd7412986eb09c6c3e492e2,

title = "The RNA polymerase 2 C-terminal domain-interacting domain of yeast Nrd1 contributes to the choice of termination pathway and couples to RNA processing by the nuclear exosome",

abstract = "Background: Distinct termination pathways for yeast RNA polymerase II (RNApII) employ proteins (Nrd1 and Rtt103) recognizing different phospho-forms of the RNApII C-terminal domain (CTD). Results: Alteration of CTD-binding specificity of Nrd1 significantly affects RNApII termination. Conclusion: Differential interaction between RNApII CTD and termination factors is crucial in choosing a termination pathway. Significance: CTD-interacting domain of Nrd1 couples termination and RNA processing by the nuclear exosome.",

author = "Heo, \{Dong Hyuk\} and Inhea Yoo and Jiwon Kong and Michael Lidschreiber and Andreas Mayer and Choi, \{Byung Yi\} and Yoonsoo Hahn and Patrick Cramer and Stephen Buratowski and Minkyu Kim",

year = "2013",

month = dec,

day = "20",

doi = "10.1074/jbc.M113.508267",

language = "English (US)",

volume = "288",

pages = "36676--36690",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "51",

}

TY - JOUR

T1 - The RNA polymerase 2 C-terminal domain-interacting domain of yeast Nrd1 contributes to the choice of termination pathway and couples to RNA processing by the nuclear exosome

AU - Heo, Dong Hyuk

AU - Yoo, Inhea

AU - Kong, Jiwon

AU - Lidschreiber, Michael

AU - Mayer, Andreas

AU - Choi, Byung Yi

AU - Hahn, Yoonsoo

AU - Cramer, Patrick

AU - Buratowski, Stephen

AU - Kim, Minkyu

PY - 2013/12/20

Y1 - 2013/12/20

N2 - Background: Distinct termination pathways for yeast RNA polymerase II (RNApII) employ proteins (Nrd1 and Rtt103) recognizing different phospho-forms of the RNApII C-terminal domain (CTD). Results: Alteration of CTD-binding specificity of Nrd1 significantly affects RNApII termination. Conclusion: Differential interaction between RNApII CTD and termination factors is crucial in choosing a termination pathway. Significance: CTD-interacting domain of Nrd1 couples termination and RNA processing by the nuclear exosome.

AB - Background: Distinct termination pathways for yeast RNA polymerase II (RNApII) employ proteins (Nrd1 and Rtt103) recognizing different phospho-forms of the RNApII C-terminal domain (CTD). Results: Alteration of CTD-binding specificity of Nrd1 significantly affects RNApII termination. Conclusion: Differential interaction between RNApII CTD and termination factors is crucial in choosing a termination pathway. Significance: CTD-interacting domain of Nrd1 couples termination and RNA processing by the nuclear exosome.

UR - https://www.scopus.com/pages/publications/84890905264

UR - https://www.scopus.com/inward/citedby.url?scp=84890905264&partnerID=8YFLogxK

U2 - 10.1074/jbc.M113.508267

DO - 10.1074/jbc.M113.508267

M3 - Article

C2 - 24196955

AN - SCOPUS:84890905264

SN - 0021-9258

VL - 288

SP - 36676

EP - 36690

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 51

ER -

The RNA polymerase 2 C-terminal domain-interacting domain of yeast Nrd1 contributes to the choice of termination pathway and couples to RNA processing by the nuclear exosome

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this