Molecular characterisation of RecQ homologues in Arabidopsis thaliana
AUTOR(ES)
Hartung, Frank
FONTE
Oxford University Press
RESUMO
Members of the RecQ family of DNA helicases are involved in processes linked to DNA replication, DNA recombination and gene silencing. RecQ homologues of various animals have been described recently. Here, for the first time for plants, we characterised cDNAs of all in all six different RecQ-like proteins that are expressed to different extents in Arabidopsis thaliana. Surprisingly, three of these proteins are small in size [AtRecQl1, AtRecQl2, AtRecQl3—606, 705 and 713 amino acids (aa), respectively], whereas the two bigger proteins result from a duplication event during plant evolution [AtRecQl4A and AtRecQl4B—1150 and 1182 aa, respectively]. Another homologue (AtRecQsim, 858 aa) most probably arose by insertion of an unrelated sequence within its helicase domain. The presence of these homologues demonstrates the conservation of RecQ family functions in higher eukaryotes. We also detected a small gene (AtWRNexo) encoding 285 aa which, being devoid of any RecQ-like helicase domain, reveals a striking homology to the exonuclease domain of human Werner protein, a prominent RecQ helicase of larger size. By means of the two-hybrid assay we were able to detect an interaction between AtWRNexo and AtRecQl2, indicating that activities that reside in a single protein chain in mammals might in plants be complemented in trans.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=113147Documentos Relacionados
- Molecular characterisation of two paralogous SPO11 homologues in Arabidopsis thaliana
- Substrate-specific inhibition of RecQ helicase
- Domain mapping of Escherichia coli RecQ defines the roles of conserved N- and C-terminal regions in the RecQ family
- Escherichia coli RecQ protein is a DNA helicase
- Escherichia coli RecQ protein is a DNA helicase.
