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Title: The FIP-1 like polyadenylation factor in trypanosomes and the structural basis for its interaction with CPSF30

Journal Article · · Biochemical and Biophysical Research Communications
;  [1];  [1]
  1. INGEBI-CONICET, Vta. de Obligado 2490, 2P, CP 1428, 1428 Buenos Aires (Argentina)

In trypanosomes transcription is polycistronic and individual mRNAs are generated by a trans-splicing/polyadenylation coupled reaction. We identified a divergent trypanosome FIP1-like, a factor required for mRNA 3' end formation from yeasts to human. Here we showed that it is a nuclear protein with a speckled distribution essential for trypanosome viability. A strong interaction was found between TcFIP1-like and TcCPSF30, a component of the polyadenylation complex. We determined the specific amino acids in each protein involved in the interaction. Significant differences were found between the trypanosome interaction surface and its human counterpart. Although CPSF30/FIP1 interaction is known in other organisms, this is the first report mapping the interaction surface at the amino acid level.

OSTI ID:
21255942
Journal Information:
Biochemical and Biophysical Research Communications, Vol. 380, Issue 4; Other Information: DOI: 10.1016/j.bbrc.2009.01.182; PII: S0006-291X(09)00242-3; Copyright (c) 2009 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
Country of Publication:
United States
Language:
English

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