![]()
|
|
||||||||
J. Biol. Chem., Vol. 278, Issue 21, 18884-18894, May 23, 2003
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||


From the Instituto de Investigaciones Biotecnológicas-Instituto Tecnológico de Chascomús, CONICET-UNSAM, 1650 San Martín, Provincia de Buenos Aires, Argentina
Trypanosomes, protozoan parasites from the order Kinetoplastida, have to deal with environmental changes during the interaction with their hosts. Trypanosoma cruzi, the causative agent of Chagas' disease, uses post-transcriptional mechanisms to regulate gene expression. However, few RNA-binding proteins involved in mRNA turnover control have been identified to date. In this work, an RNA recognition motif (RRM)-type RNA-binding protein family named T. cruzi RNA-binding protein (TcRBP) and composed of at least six members was identified. The genomic organization of four members revealed a head to tail arrangement within a region of 15 kilobase pairs. TcRBP members have a common RRM and different auxiliary domains with a high content of glycine, glutamine, and histidine residues within their N- and C-terminal regions. TcRBPs differ in their expression patterns as well as in their homoribopolymer binding interaction in vitro, although they preferentially recognize poly(U) and poly(G) RNAs. An interesting observation was the relaxed RNA-binding interactions with several trypanosome transcripts in vitro. In contrast, co-immunoprecipitation experiments of TcRBP-containing ribonucleoprotein complexes formed in vivo revealed a highly restricted binding interaction with specific RNAs. Several TcRBP-containing complexes are stage-specific and, in some cases, bear the poly(A)-binding protein TcPABP1. Altogether, these results suggest that TcRBPs might be modulated in vivo, to favor or preclude the interaction with specific transcripts in a developmentally regulated manner.
Received for publication, February 19, 2003
![]()
CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati What's this?
This article has been cited by other articles:
![]() |
A. M. Estevez The RNA-binding protein TbDRBD3 regulates the stability of a specific subset of mRNAs in trypanosomes Nucleic Acids Res., August 1, 2008; 36(14): 4573 - 4586. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. V. Jager, J. G. De Gaudenzi, A. Cassola, I. D'Orso, and A. C. Frasch Inaugural Article: mRNA maturation by two-step trans-splicing/polyadenylation processing in trypanosomes PNAS, February 13, 2007; 104(7): 2035 - 2042. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. Huang, J. Hwang, S. D. Sharma, M. R. S. Hargittai, Y. Chen, J. J. Arnold, K. D. Raney, and C. E. Cameron Hepatitis C Virus Nonstructural Protein 5A (NS5A) Is an RNA-binding Protein J. Biol. Chem., October 28, 2005; 280(43): 36417 - 36428. [Abstract] [Full Text] [PDF] |
||||
![]() |
B. Mittra and D. S. Ray Presence of a Poly(A) Binding Protein and Two Proteins with Cell Cycle-Dependent Phosphorylation in Crithidia fasciculata mRNA Cycling Sequence Binding Protein II Eukaryot. Cell, October 1, 2004; 3(5): 1185 - 1197. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. MILONE, J. WILUSZ, and V. BELLOFATTO Characterization of deadenylation in trypanosome extracts and its inhibition by poly(A)-binding protein Pab1p RNA, March 1, 2004; 10(3): 448 - 457. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |