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Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II.

Publication ,  Journal Article
Carty, SM; Goldstrohm, AC; Suñé, C; Garcia-Blanco, MA; Greenleaf, AL
Published in: Proc Natl Acad Sci U S A
August 1, 2000

An approach for purifying nuclear proteins that bind directly to the hyperphosphorylated C-terminal repeat domain (CTD) of RNA polymerase II was developed and used to identify one human phosphoCTD-associating protein as CA150. CA150 is a nuclear factor implicated in transcription elongation. Because the hyperphosphorylated CTD is a feature of actively transcribing RNA polymerase II (Pol II), phosphoCTD (PCTD) binding places CA150 in a location appropriate for performing a role in transcription elongation-related events. Several recombinant segments of CA150 bound the PCTD. Predominant binding is mediated by the portion of CA150 containing six FF domains, compact modules of previously unknown function. In fact, small recombinant proteins containing the fifth FF domain bound the PCTD. PCTD binding is the first specific function assigned to an FF domain. As FF domains are found in a variety of nuclear proteins, it is likely that some of these proteins are also PCTD-associating proteins. Thus FF domains appear to be compact protein-interaction modules that, like WW domains, can be evolutionarily shuffled to organize nuclear function.

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Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

August 1, 2000

Volume

97

Issue

16

Start / End Page

9015 / 9020

Location

United States

Related Subject Headings

  • Transcriptional Elongation Factors
  • Trans-Activators
  • RNA Polymerase II
  • Protein Binding
  • Phosphorylation
  • Humans
  • Hela Cells
  • HeLa Cells
  • DNA Primers
  • Cell Nucleus
 

Citation

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Carty, S. M., Goldstrohm, A. C., Suñé, C., Garcia-Blanco, M. A., & Greenleaf, A. L. (2000). Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II. Proc Natl Acad Sci U S A, 97(16), 9015–9020. https://doi.org/10.1073/pnas.160266597
Carty, S. M., A. C. Goldstrohm, C. Suñé, M. A. Garcia-Blanco, and A. L. Greenleaf. “Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II.Proc Natl Acad Sci U S A 97, no. 16 (August 1, 2000): 9015–20. https://doi.org/10.1073/pnas.160266597.
Carty SM, Goldstrohm AC, Suñé C, Garcia-Blanco MA, Greenleaf AL. Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II. Proc Natl Acad Sci U S A. 2000 Aug 1;97(16):9015–20.
Carty, S. M., et al. “Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II.Proc Natl Acad Sci U S A, vol. 97, no. 16, Aug. 2000, pp. 9015–20. Pubmed, doi:10.1073/pnas.160266597.
Carty SM, Goldstrohm AC, Suñé C, Garcia-Blanco MA, Greenleaf AL. Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II. Proc Natl Acad Sci U S A. 2000 Aug 1;97(16):9015–9020.
Journal cover image

Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

August 1, 2000

Volume

97

Issue

16

Start / End Page

9015 / 9020

Location

United States

Related Subject Headings

  • Transcriptional Elongation Factors
  • Trans-Activators
  • RNA Polymerase II
  • Protein Binding
  • Phosphorylation
  • Humans
  • Hela Cells
  • HeLa Cells
  • DNA Primers
  • Cell Nucleus