Structural Studies of FF Domains of the Transcription Factor CA150 Provide Insights into the Organization of FF Domain Tandem Arrays

JM Murphy; DF Hansen; S Wiesner; DR Muhandiram; M Borg; MJ Smith; F Sicheri; LE Kay; JD Forman-Kay; T Pawson

Journal article

Structural Studies of FF Domains of the Transcription Factor CA150 Provide Insights into the Organization of FF Domain Tandem Arrays

JM Murphy, DF Hansen, S Wiesner, DR Muhandiram, M Borg, MJ Smith, F Sicheri, LE Kay, JD Forman-Kay, T Pawson

Journal of Molecular Biology | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | Published : 2009

DOI: 10.1016/j.jmb.2009.08.049

Abstract

FF domains are poorly understood protein interaction modules that are present within eukaryotic transcription factors, such as CA150 (TCERG-1). The CA150 FF domains have been shown to mediate interactions with the phosphorylated C-terminal domain of RNA polymerase II (phosphoCTD) and a multitude of transcription factors and RNA processing proteins, and may therefore have a central role in organizing transcription. FF domains occur in tandem arrays of up to six domains, although it is not known whether they adopt higher-order structures. We have used the CA150 FF1 + FF2 domains as a model system to examine whether tandem FF domains form higher-order structures in solution using NMR spectrosco..

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University of Melbourne Researchers

James Murphy Author

Grants

Awarded by Canadian Institutes of Health Research

Funding Acknowledgements

We thank Dr Soren Kristensen (University of Copenhagen) for his role in developing the relaxation data analysis program FuDA. Dr Remco Sprangers is thanked for helpful discussions and computational wizardry. We thank Dr Xiaon-dn Chen for sharing data before publication. Support was gratefully received by J.M.M. (C.J. Martin Fellowship of the National Health and Medical Research Council of Australia, Grant 305546), D.F.H. (post-doctoral fellowship from the Canadian Institutes of Health Research (CIHR)), M.B. (post-doctoral fellowships from the CIHR Training Program in Protein Folding and Swedish-America Foundation), and M.J.S. (postgraduate scholarship from Natural Sciences and Engineering Research Council (NSERC), Canada). This work was supported by grants from the National Cancer Institute of Canada (NCIC) and CIHR to F.S. (CIHR grant #MOP-36399), J.D.F.-K. and T.P. (CIHR grant #MOP-6849) and Genome Canada to T.P.