| Summary: | <p>Abstract</p> <p>Background</p> <p>The periodontal pathogen <it>Porphyromonas gingivalis </it>is an obligate anaerobe that requires heme for growth. To understand its heme acquisition mechanism, we focused on a hemin-binding protein (HBP35 protein), possessing one thioredoxin-like motif and a conserved C-terminal domain, which are proposed to be involved in redox regulation and cell surface attachment, respectively.</p> <p>Results</p> <p>We observed that the <it>hbp35 </it>gene was transcribed as a 1.1-kb mRNA with subsequent translation resulting in three proteins with molecular masses of 40, 29 and 27 kDa in the cytoplasm, and one modified form of the 40-kDa protein on the cell surface. A recombinant 40-kDa HBP35 exhibited thioredoxin activity <it>in vitro </it>and mutation of the two putative active site cysteine residues abolished this activity. Both recombinant 40- and 27-kDa proteins had the ability to bind hemin, and growth of an <it>hbp35 </it>deletion mutant was substantially retarded under hemin-depleted conditions compared with growth of the wild type under the same conditions.</p> <p>Conclusion</p> <p><it>P. gingivalis </it>HBP35 exhibits thioredoxin and hemin-binding activities and is essential for growth in hemin-depleted conditions suggesting that the protein plays a significant role in hemin acquisition.</p>
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