TAILIEUCHUNG - Báo cáo khoa học: Identification of a copper-repressible C-type heme protein of Methylococcus capsulatus (Bath) A member of a novel group of the bacterial di-heme cytochrome c peroxidase family of proteins

Genomic sequencing of the methanotrophic bacterium,Methylococcus cap-sulatus (Bath), revealed an open reading frame (MCA2590) immediately upstream of the previously described mopEgene (MCA2589). Sequence analyses of the deduced amino acid sequence demonstrated that the MCA2590-encoded protein shared significant, but restricted, sequence simi-larity to the bacterial di-heme cytochrome c peroxidase (BCCP) family of proteins. | iFEBS Journal Identification of a copper-repressible C-type heme protein of Methylococcus capsulatus Bath A member of a novel group of the bacterial di-heme cytochrome c peroxidase family of proteins Odd A. Karlsen1 Louise Kindingstad1 Solveig M. Angelskar1 Live J. Bruseth1 Daniel Straume1 Pal Puntervoll2 Anne Fjellbirkeland1 Johan R. Lillehaug1 and Harald B. Jensen1 1 Department of Molecular Biology University of Bergen Norway 2 ComputationalBiology Unit Bergen Centre for ComputationalScience Norway Keywords cell surface exposed copper regulated cytochrome c peroxidase methanotrophs Methylococcus capsulatus Correspondence O. A. Karlsen Department of Molecular Biology University of Bergen HIB Thormohlensgt. 55 5020 Bergen Norway Fax 47 555 89683 Tel 47 555 84372 E-mail Received 27 July 2005 revised 7 October 2005 accepted 17 October 2005 doi Genomic sequencing of the methanotrophic bacterium Methylococcus cap-sulatus Bath revealed an open reading frame MCA2590 immediately upstream of the previously described mopE gene MCA2589 . Sequence analyses of the deduced amino acid sequence demonstrated that the MCA2590-encoded protein shared significant but restricted sequence similarity to the bacterial di-heme cytochrome c peroxidase BCCP family of proteins. Two putative C-type heme-binding motifs were predicted and confirmed by positive heme staining. Immunospecific recognition and biotinylation of whole cells combined with MS analyses confirmed expression of MCA2590 in M. capsulatus as a protein noncovalently associated with the cellular surface of the bacterium exposed to the cell exterior. Similar to MopE expression of MCA2590 is regulated by the bioavailability of copper and is most abundant in M. capsulatus cultures grown under low copper conditions thus indicating an important physiological role under these growth conditions. MCA2590 is distinguished from previously characterized members of the BCCP family by .

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