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Characterization of a chaperone ClpB homologue of Paracoccidioides brasiliensis
Author(s) -
Jesuino Rosália S. A.,
Azevedo Maristela O.,
Felipe M. Sueli S.,
Pereira Maristela,
de Almeida Soares Célia M.
Publication year - 2002
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.888
Subject(s) - clpb , biology , paracoccidioides brasiliensis , chaperone (clinical) , open reading frame , gene , genetics , microbiology and biotechnology , peptide sequence , biochemistry , heat shock protein , medicine , pathology
We report the cloning and sequence analysis of a genomic clone encoding a Paracoccidioides brasiliensis ClpB chaperone homologue ( Pb ClpB). The clpb gene was identified in a λ Dash II library. Sequencing of Pbclpb revealed a long open reading frame capable of encoding a 792 amino acid, 87.9 kDa protein, pI of 5.34. The predicted polypeptide contains several consensus motifs of the ClpB proteins. Canonical sequences such as two putative nucleotide‐binding sites, chaperonins ClpA/B signatures and highly conserved casein kinase phosphorylation domains are present. ClpB is 69% to 49% identical to members of the ClpB family from several organisms from prokaryotes to eukaryotes. The transcript of Pb clpB was detected as a mRNA species of 3.0 kb, preferentially expressed in the yeast parasitic phase of the fungus. A 89 kDa protein was also detected in yeast cells of P. brasiliensis . The sequence of the clpb gene and the deduced ClpB protein have been submitted to GenBank under Accession No. AF449501. Copyright © 2002 John Wiley & Sons, Ltd.