Characterization of a chaperone ClpB homologue of Paracoccidioides brasiliensis

Yeast. 2002 Aug;19(11):963-72. doi: 10.1002/yea.888.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • Endopeptidase Clp
  • Escherichia coli Proteins*
  • Heat-Shock Proteins / chemistry*
  • Heat-Shock Proteins / genetics*
  • Heat-Shock Proteins / metabolism
  • Heat-Shock Response
  • Humans
  • Molecular Sequence Data
  • Paracoccidioides / genetics
  • Paracoccidioides / growth & development
  • Paracoccidioides / metabolism*
  • Sequence Alignment
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid

Substances

  • Escherichia coli Proteins
  • Heat-Shock Proteins
  • Endopeptidase Clp
  • ClpB protein, E coli

Associated data

  • GENBANK/AF449501