This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Frustaci, J M Articles by O'Brian, M R Search for Related Content PubMed PubMed Citation Articles by Frustaci, J M Articles by O'Brian, M R Agricola Articles by Frustaci, J M Articles by O'Brian, M R

Next Article 

Appl Environ Microbiol. 1993 August; 59(8): 2347-2351

Analysis of the Bradyrhizobium japonicum hemH gene and its expression in Escherichia coli.

Department of Biochemistry, State University of New York, Buffalo 14214.

ABSTRACT

Complementation analysis showed that the Bradyrhizobium japonicum hemH gene was both necessary and sufficient to rescue mutant strains I110ek4 and I110bk2 in trans with respect to hemin auxotrophy, protoporphyrin accumulation, and the deficiency in ferrochelatase activity. The B. japonicum hemH gene was expressed in an Escherichia coli T7 expression system and yielded a 39-kDa protein, which was consistent with the predicted size of the deduced product. The overexpressed protein was purified and shown to contain ferrochelatase activity, thereby demonstrating that the hemH gene encodes ferrochelatase. When expressed from the lac promoter, the B. japonicum hemH gene was able to complement the enzyme activity of a ferrochelatase-defective E. coli mutant, and it also conferred hemin prototrophy on those cells. These latter findings confirm the identity of the hemH gene product and demonstrate that B. japonicum ferrochelatase can interact with the E. coli heme synthesis enzymes for heme formation in complemented cells.

This article has been cited by other articles:

• Chauhan, S., O'Brian, M. R. (1995). A Mutant Bradyrhizobium japonicum [IMAGE]-Aminolevulinic Acid Dehydratase with an Altered Metal Requirement Functions in Situ for Tetrapyrrole Synthesis in Soybean Root Nodules. J. Biol. Chem. 270: 19823-19827 [Abstract] [Full Text]  
• Frustaci, J. M., Sangwan, I., O'Brian, M. R. (1995). gsa1 Is a Universal Tetrapyrrole Synthesis Gene in Soybean and Is Regulated by a GAGA Element. J. Biol. Chem. 270: 7387-7393 [Abstract] [Full Text]