Previous Article | Next Article ![]()
Molecular and Cellular Biology, November 2005, p. 9209-9220, Vol. 25, No. 21
0270-7306/05/$08.00+0 doi:10.1128/MCB.25.21.9209-9220.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Sandra L. Martin,2 and
M. Carmen Thomas1*
Departamento de Biología Molecular, Instituto de Parasitología y Biomedicina "López Neyra," CSIC, 18100 Granada, Spain,1 Department of Cell and Developmental Biology, University of Colorado School of Medicine, Aurora, Colorado 800452
Received 11 January 2005/ Returned for modification 4 April 2005/ Accepted 5 August 2005
L1Tc, a non-long terminal repeat retrotransposon from Trypanosoma cruzi, is a 4.9-kb actively transcribed element which contains a single open reading frame coding for the machinery necessary for its autonomous retrotransposition. In this paper, we analyze the protein encoded by the L1Tc 3' region, termed C2-L1Tc, which contains two zinc finger motifs similar to those present in the TFIIIA transcription factor family. C2-L1Tc binds nucleic acids with different affinities, such that RNA > tRNA > single-stranded DNA > double-stranded DNA, without any evidence for sequence specificity. C2-L1Tc also exhibits nucleic acid chaperone activity on different DNA templates that may participate in the mechanism of retrotransposition of the element. C2-L1Tc promotes annealing of complementary oligonucleotides, prevents melting of perfect DNA duplexes, and facilitates the strand exchange between DNAs to form the most stable duplex DNA in competitive displacement assays. Mapping of regions of C2-L1Tc using specific peptides showed that nucleic acid chaperone activity required a short basic sequence accompanied by a zinc finger motif or by another basic region such as RRR. Thus, a short basic polypeptide containing the two C2H2 motifs promotes formation of the most stable duplex DNA at a concentration only three times higher than that required for C2-L1Tc.
Present address: Departments of Human Genetics and Internal Medicine, University of Michigan Medical School, Ann Arbor, MI 48109-0618.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»