Characterization of a chaperone ClpB homologue of Paracoccidioides brasiliensis
| Autor: | Maristela Pereira, Rosália Santos Amorim Jesuino, Célia Maria de Almeida Soares, M. Sueli S. Felipe, Maristela O. Azevedo |
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| Rok vydání: | 2002 |
| Předmět: |
Sequence analysis
Molecular Sequence Data Bioengineering Sequence alignment Biology Applied Microbiology and Biotechnology Biochemistry Chaperonin Genetics Humans Amino Acid Sequence Cloning Molecular Peptide sequence Heat-Shock Proteins Paracoccidioides brasiliensis Base Sequence Sequence Homology Amino Acid Escherichia coli Proteins Paracoccidioides Endopeptidase Clp Sequence Analysis DNA biology.organism_classification Open reading frame Chaperone (protein) biology.protein CLPB Sequence Alignment Heat-Shock Response Biotechnology |
| Zdroj: | Yeast (Chichester, England). 19(11) |
| ISSN: | 0749-503X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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