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Cloning and expression of a Porphyromonas gingivalis gene for protoporphyrinogen oxidase by complementation of a hemG mutant of Escherichia coli.
- Source :
-
Oral Microbiology & Immunology . Oct2002, Vol. 17 Issue 5, p290-295. 6p. - Publication Year :
- 2002
-
Abstract
- Porphyromonas gingivalis , a bacterium implicated in periodontal pathogenesis, has a growth requirement for iron protoporphyrin IX. By complementation with a P. gingivalis 381 chromosomal DNA library, we were able to isolate a clone that enhanced the poor growth of a hemG mutant of Escherichia coli . The DNA sequence analysis of this clone revealed three open reading frames (ORFs). ORF3 encoded a protein of 466 amino acids with a calculated molecular weight of 51 695 Da. The deduced amino acid sequence of the ORF3 gene had significant similarity to sequences of protoporphyrinogen oxidase (PPO) from Myxococcus xanthus (30% identical residues). When the ORF3 gene was overexpressed in E. coli , the extract had much higher PPO activity than a control extract, and this activity was inhibited by acifluorfen, a specific inhibitor of PPO. Thus, ORF3 was named PgHemG. Furthermore, several porphyrin-related genes, including hemD , hemN and hemH , were identified in the data bases on the websites available on-line. We postulated that a porphyrin biosynthetic pathway to heme from preuroporphyrin may be conserved in P. gingivalis . [ABSTRACT FROM AUTHOR]
- Subjects :
- *PORPHYROMONAS gingivalis
*OXIDASES
*IRON proteins
*ESCHERICHIA coli
Subjects
Details
- Language :
- English
- ISSN :
- 09020055
- Volume :
- 17
- Issue :
- 5
- Database :
- Academic Search Index
- Journal :
- Oral Microbiology & Immunology
- Publication Type :
- Academic Journal
- Accession number :
- 7418769
- Full Text :
- https://doi.org/10.1034/j.1399-302X.2002.170505.x