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Metabolism of cyclohexane carboxylic acid by the photosynthetic bacterium Rhodopseudomonas palustris (1995)

Küver, J. ; Xu, Yuhong ; Gibson, Jane

Springer

Archives of microbiology 164 (1995), S. 337-345

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ISSN: 1432-072X

Keywords: Key wordsRhodopseudomonas palustris ; Aryl-CoA ligase ; Thioesterase ; Anaerobic degradation of aromatic compounds ; Cyclohexane carboxylate

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Cyclohexane carboxylate supported relatively rapid growth (doubling times 7–8 h) of Rhodopseudomonas palustris under oxic or photosynthetic conditions, but did not serve as a substrate for either of the known aromatic CoA ligases. A CoA ligase that thioesterifies cyclohexane carboxylate was partially purified and did not cross react immunologically with the two CoA ligases purified previously from this bacterium. Crude extracts of R. palustris cells grown with a range of aromatic or alicyclic acids contained a dehydrogenase that reacted with cyclohexane carboxyl-CoA or cyclohex-1-ene carboxyl-CoA, using 2,6-dichlorophenolindophenol or ferricenium ion as electron carrier. This activity was not detected in extracts of adipate-, glutamate-, or succinate-grown cells. No oxidation or reduction of nonesterified cyclohexane carboxylate or cyclohexene carbocylate was detected in extracts of cells grown with aromatic or aliphatic substrates, neither aerobically nor anaerobically. A constitutively expressed thioesterase that hydrolyzed cyclohexane carboxyl-CoA and also some alicyclic and aliphatic CoA derivatives was purified and characterized. The enzyme had little or no activity on benzoyl-CoA or 4-hydroxybenzoyl-CoA. The presence of a thioesterase that effectively hydrolyzes cyclohexane carboxyl-CoA suggests that transient production of cyclohexane carboxylate is a physiological response to temporary excess of reductant during metabolism of aromatic compounds.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/s002030050272

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Chromatin structure changes suggest a compensatory response to c-myc gene amplification in malignant fibrous histiocytoma (1992)

Gibson, Jane S. ; Croker, Byron P.

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 49 (1992), S. 148-156

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ISSN: 0730-2312

Keywords: c-myc transcription ; DNAse I hypersensitivity ; oncogenes ; sarcomas ; tumor cell lines ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: Changes in chromatin structure as determined from DNAse I hypersensitive site analysis are associated with c-myc amplification and increased transcript/protein levels in malignant fibrous histiocytoma (MFH) cell lines. A DNAse I hypersensitive site near the PO promoter region was observed in one MFH cell line (UR HCL 1), and in normal fibroblasts (HFF), but not in an MFH cell line with an amplified c-myc gene (P3C). A DNAse I hypersensitive site exclusive to P3C amplified c-myc was identified slightly 3′ of exon one. No alterations in c-myc DNAse I hypersensitive site patterns were observed in HFF fibroblasts following serum release, when peak levels of c-myc transcript were induced. DNAse I hypersensitive site patterns associated with gene amplification may reflect a compensatory response by P3C cells to an abundance of c-myc transcript. Furthermore, elevated levels of protein in P3C cells provide additional evidence that amplified c-myc is an oncogene in MFHs.

Additional Material: 5 Ill.