Journal of Bacteriology, May 1999, p. 2914-2921, Vol. 181, No. 9
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Laboratory of Molecular Biotechnology,
Received 3 September 1998/Accepted 10 February 1999
The polyhydroxyalkanoic acid (PHA) granule-associated 16-kDa
protein (GA16 protein) of Paracoccus denitrificans was
identified, and its corresponding gene was cloned and analyzed at the
molecular level. The N-terminal amino acid sequence of GA16 protein
revealed that its structural gene is located downstream from the PHA
synthase gene (phaCPd) cloned recently (S. Ueda, T. Yabutani, A. Maehara, and T. Yamane, J. Bacteriol.
178:774-779, 1996). Gene walking around phaCPd
revealed two new open reading frames (ORFs) possibly related to PHA
synthesis, one of which was the phaPPd gene,
encoding GA16 protein, and the other was the
phaRPd gene, encoding a protein that is
putatively involved in the regulation of the expression of
phaPPd. Overproduction of PhaPPd
was observed in Escherichia coli carrying
phaPPd, but the overproduction was not observed in the presence of phaRPd. Coexpression of
phaPPd and PHA biosynthesis genes in E. coli caused increases in both the number of
poly-(3-hydroxybutyric acid) (PHB) granules and PHB content and caused
decreases in both the size of the granules and the molecular weight of
PHB. GA16 protein was considered a phasin protein. The
phaRPd gene had significant similarities to
stdC, a possible transcriptional factor of Comamonas testosteroni, as well as to other ORFs of unknown function
previously found in other PHA-synthetic bacteria.
*
Corresponding author. Mailing address: Laboratory of
Molecular Biotechnology, Division of Molecular Cell Mechanisms,
Department of Biological Mechanisms and Functions, Graduate School of
Bio- and Agro-Sciences, Nagoya University, Furo-cho, Chikusa-ku,
Nagoya 464-8601, Japan. Phone: 81-52-789-4142. Fax:
81-52-789-4145. E-mail: yamanetu{at}agr.nagoya-u.ac.jp.
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