Abstract:
:The N-terminal amino acid sequence of the polyhydroxyalkanoic acid (PHA) granule-associated M(r)-15,500 protein of Rhodococcus ruber (the GA14 protein) was analyzed. The sequence revealed that the corresponding structural gene is represented by open reading frame 3, encoding a protein with a calculated M(r) of 14,175 which was recently localized downstream of the PHA synthase gene (U. Pieper and A. Steinbüchel, FEMS Microbiol. Lett. 96:73-80, 1992). A recombinant strain of Escherichia coli XL1-Blue carrying the hybrid plasmid (pSKXA10*) with open reading frame 3 overexpressed the GA14 protein. The GA14 protein was subsequently purified in a three-step procedure including chromatography on DEAE-Sephacel, phenyl-Sepharose CL-4B, and Superose 12. Determination of the molecular weight by gel filtration as well as electron microscopic studies indicates that a tetrameric structure of the recombinant, native GA14 protein is most likely. Immunoelectron microscopy demonstrated a localization of the GA14 protein at the periphery of PHA granules as well as close to the cell membrane in R. ruber. Investigations of PHA-leaky and PHA-negative mutants of R. ruber indicated that expression of the GA14 protein depended strongly on PHA synthesis.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Pieper-Fürst U,Madkour MH,Mayer F,Steinbüchel Adoi
10.1128/jb.176.14.4328-4337.1994subject
Has Abstractpub_date
1994-07-01 00:00:00pages
4328-37issue
14eissn
0021-9193issn
1098-5530journal_volume
176pub_type
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journal_title:Journal of bacteriology
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pub_type: 杂志文章
doi:10.1128/JB.158.2.551-561.1984
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pub_type: 杂志文章
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更新日期:1971-02-01 00:00:00