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Gene products from Bacillus megateri...

McCool, Gabriel J.

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Gene products from Bacillus megaterium involved in the metabolism of polyhydroxyalkanoic acid (PHA) and the biogenesis of PHA inclusion-bodies.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Gene products from Bacillus megaterium involved in the metabolism of polyhydroxyalkanoic acid (PHA) and the biogenesis of PHA inclusion-bodies./
Author:	McCool, Gabriel J.
Description:	191 p.
Notes:	Director: Maura C. Cannon.
Contained By:	Dissertation Abstracts International62-04B.
Subject:	Biology, Genetics. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3012163
ISBN:	0493219773

Gene products from Bacillus megaterium involved in the metabolism of polyhydroxyalkanoic acid (PHA) and the biogenesis of PHA inclusion-bodies.
McCool, Gabriel J.

Gene products from Bacillus megaterium involved in the metabolism of polyhydroxyalkanoic acid (PHA) and the biogenesis of PHA inclusion-bodies. - 191 p.

Director: Maura C. Cannon.

Thesis (Ph.D.)--University of Massachusetts Amherst, 2001.

Polyhydroxyalkanoates (PHAs) comprise a family of macromolecules produced by many bacteria as a carbon and energy reserve and are perceived to have commercial potential as biodegradable thermoplastics. To investigate the biogenesis of PHA inclusion-bodies and the functions of inclusion-body proteins from <italic> Bacillus megaterium</italic> strain 11561, we identified and cloned a 7.9 kb DNA fragment harboring five genes, <italic>phaP, -Q, -R, -B</italic>, and <italic> -C</italic> specifying proteins having known or putative functions in PHA metabolism and/or inclusion-body biogenesis. Sequence similarities to known <italic> pha</italic> genes identified <italic>phaB</italic> and <italic>-C</italic> as specifying acetoacetyl-CoA reductase and PHA synthase, respectively. Putative proteins encoded by <italic>phaP, -Q</italic>, and <italic>-R</italic> were not ascribed functions due to lack of significant similarities to known proteins. Both the functionality of the <italic>pha</italic> gene cluster with respect to PHA accumulation and the transcriptional organization of the genes were determined. Subsequent studies were carried out to further investigate functions of <italic>phaP, -Q</italic>, and <italic>-R</italic>.

ISBN: 0493219773Subjects--Topical Terms:

1017730
Biology, Genetics.

Gene products from Bacillus megaterium involved in the metabolism of polyhydroxyalkanoic acid (PHA) and the biogenesis of PHA inclusion-bodies.
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245 1 0 $a Gene products from Bacillus megaterium involved in the metabolism of polyhydroxyalkanoic acid (PHA) and the biogenesis of PHA inclusion-bodies.
300 $a 191 p.
500 $a Director: Maura C. Cannon.
500 $a Source: Dissertation Abstracts International, Volume: 62-04, Section: B, page: 1713.
502 $a Thesis (Ph.D.)--University of Massachusetts Amherst, 2001.
520 $a Polyhydroxyalkanoates (PHAs) comprise a family of macromolecules produced by many bacteria as a carbon and energy reserve and are perceived to have commercial potential as biodegradable thermoplastics. To investigate the biogenesis of PHA inclusion-bodies and the functions of inclusion-body proteins from <italic> Bacillus megaterium</italic> strain 11561, we identified and cloned a 7.9 kb DNA fragment harboring five genes, <italic>phaP, -Q, -R, -B</italic>, and <italic> -C</italic> specifying proteins having known or putative functions in PHA metabolism and/or inclusion-body biogenesis. Sequence similarities to known <italic> pha</italic> genes identified <italic>phaB</italic> and <italic>-C</italic> as specifying acetoacetyl-CoA reductase and PHA synthase, respectively. Putative proteins encoded by <italic>phaP, -Q</italic>, and <italic>-R</italic> were not ascribed functions due to lack of significant similarities to known proteins. Both the functionality of the <italic>pha</italic> gene cluster with respect to PHA accumulation and the transcriptional organization of the genes were determined. Subsequent studies were carried out to further investigate functions of <italic>phaP, -Q</italic>, and <italic>-R</italic>.
520 $a PhaP was established as a major PHA inclusion-body associated protein and was shown to localize to inclusion-bodies in living cells. Further, we demonstrated a phasin-like role for this protein due to its affect on the formation of PHA inclusion-bodies. In addition, our data is consistent with PhaP functioning as a storage protein, implying that the role of PHA inclusion-bodies may be that of a reserve of amino acids in addition to reduced carbon. Regulation of <italic>phaP</italic> was influenced by PhaQ We showed that PhaQ is a transcriptional repressor of <italic>phaP</italic>.
520 $a Moreover, we demonstrated the binding of PhaQ to inclusion-bodies, suggesting that its mode of regulation may involve its localization. Similarly, we showed that PhaR is bound to PHA inclusion-bodies. Our data demonstrated the requirement of <italic>phaR</italic> for PHA accumulation <italic>in vivo</italic> and that both PhaC and PhaR were necessary for PHA synthase activity <italic> in vitro</italic>. Evidence suggests that PHA synthase from strain 11561 can exist in an active or inactive state and that this state is either directly or indirectly influenced by PhaR. A working model is proposed to describe the roles of PhaP, -Q and -R in the metabolism of PHA and biogenesis of PHA inclusion-bodies.
590 $a School code: 0118.
650 4 $a Biology, Genetics. $3 1017730
650 4 $a Biology, Microbiology. $3 1017734
650 4 $a Biology, Molecular. $3 1017719
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