Characterization of a chaperone ClpB homologue of Paracoccidioides brasiliensis.
We report the cloning and sequence analysis of a genomic clone encoding a Paracoccidioides brasiliensis ClpB chaperone homologue (PbClpB). The clpb gene was identified in a lambda 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 PbclpB 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.
Laboratório de Biologia Molecular, Instituto de Ciências Biológicas, Universidade Federal de Goiás, ICB II, Campus II, 74001-970, Goiânia, Goiás, Brazil.
Rosália S A
RS
Jesuino
Maristela O
MO
Azevedo
M Sueli S
MS
Felipe
Maristela
M
Pereira
Célia M
CM
De Almeida Soares
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D049071:Endopeptidase Clp; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D018869:Heat-Shock Response; D006801:Humans; D008969:Molecular Sequence Data; D010228:Paracoccidioides / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D049071:Endopeptidase Clp; C069775:ClpB protein, E coli