Catabolite repression of protoporphyrin IX biosynthesis in <i>Escherichia coli</i> K‐12

Poulson, Rozanne; Whitlow, Karen J.; Polglase, W. J.

doi:10.1016/0014-5793(76)80092-0

Cited by 19 publications

(8 citation statements)

References 10 publications

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“…Addition of cAMP to cells growing in the presence of glucose has also been shown to elevate the synthesis of some tricarboxylic acid enzymes (18) and cytochromes (5), as well as increase the efficiency of oxidative phosphorylation (16). Furthermore, heme biosynthesis is also under the control of this mechanism (41). Hence, although it is shown in this work that both CAP and cAMP are required for the activity of the VHb promoter, it is not clear whether this is a direct or indirect effect.…”

Section: Discussionmentioning

confidence: 99%

Characterization of the oxygen-dependent promoter of the Vitreoscilla hemoglobin gene in Escherichia coli

Khosla

Bailey

1989

J Bacteriol

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The gene coding for the VitreoscUla hemoglobin (VHb) molecule has been cloned and functionally expressed in Escherichia coli. By using a plasmid-encoded gene as well as single-copy integrants, the oxygen-dependent VHb gene (VHb) promoter was shown to be functional in E. coli. The promoter was maximally induced under microaerobic conditions (dissolved oxygen levels of less than 2% air saturation). Direct analysis of mRNA levels as well as the use of gene fusions with lacZ showed that oxygen-dependent regulation occurred at the level of transcription. Transcriptional activity decreased substantially under anaerobic conditions, suggesting the presence of a regulatory mechanism that is maximally induced under hypoxic but not completely anaerobic conditions in E. coli. Primer extension analysis was used to identify the existence of two overlapping promoters within a 150-base-pair region upstream of the structural VHb gene. The oxygen-dependent activity of both promoters was qualitatively similar, suggesting the existence of a common mechanism by which available oxygen concentrations influence expression from the two promoters. Analysis of promoter activity in crp and cya mutants showed that both cyclic AMP and catabolite activator protein were required for full activity of the promoter. The VHb promoter contained a region of signfficant homology to the catabolite activator protein-binding site near the E. coli lac promoter.

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Section: Discussionmentioning

confidence: 99%

Characterization of the oxygen-dependent promoter of the Vitreoscilla hemoglobin gene in Escherichia coli

Khosla

Bailey

1989

J Bacteriol

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“…In yeast the enzyme is found only in association with mitochondria, and under glucoserepressed growth conditions the activity cannot be detected (1 56). As in other cases of catabolite repression, the repressive effects of glucose on protoporphyrinogen 9 oxidase are abolished by 3,5-cyclic AMP (156,325). The enzyme may be.…”

Section: Yeastmentioning

confidence: 99%

“…The yeast enzyme has a molecular weight of 180,OOO by gel filtration, and a K , of 4.8 p M (154). The rat liver enzyme has a molecular weight of 35,000 and a K,, of 1 1 pM (155).…”

Section: B Coproporphyrinogen 111 To Protoporphyrinogenmentioning

confidence: 99%

Hemes, Chlorophylls, and Related Compounds: Biosynthesis and Metabolic Regulation

Granick¹,

Beale²

1978

Advances in Enzymology - And Related Areas of Molecular Biology

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“…Evidence indicates that the appearance o f the 503 nm pigment is associated with growth condi tions leading to decreased Protox activities both in an E. coli m utant [39] and in a yeast [29]. These findings have suggested that when rapid enzymatic Protox activity is decreased or stopped, PTP IX accumulates as a result o f a slower non-Protoxmediated oxidation o f Protogen IX.…”

Section: Discussionmentioning

confidence: 99%

“…Tetrahydroporphyrins have been characterized chemically as relatively stable intermediates in the chemical autooxidation o f porphyrinogens (hexahydroporphyrins) to fully oxidized porphyrins [34], and PTP IX can be characterized by its 503 nm absorption maximum [27, 28,37], A pig ment with a 503 nm absorption maximum similar to that of PTP IX has been observed in the cyto plasmic fraction o f yeast growing anaerobically or in glucose minimal media [27,38] and in E. coli [39]. Evidence indicates that the appearance o f the 503 nm pigment is associated with growth condi tions leading to decreased Protox activities both in an E. coli m utant [39] and in a yeast [29].…”

Section: Discussionmentioning

confidence: 99%

HPLC and in vivo Spectrophotometric Detection of Porphyrins in Plant Tissues Treated with Porphyrinogenic Herbicides

Duke

Lee

1993

Zeitschrift Für Naturforschung C

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yellow cucum ber cotyledon discs approxim ated the ab so rp tio n spectra o f p ro to p o rp h y rin IX (P ro to IX). T here was also an enhanced peak n ear 503 nm . T reatm ent o f cotyledon discs w ith A L A alone generated a differ ence spectrum o f protochlorophyllide (PChlide) in co m b in atio n with M g -P roto IX or M g-P roto IX m onom ethyl ester (M g-P roto IX M E). W ith A L A a n d A F in co m b in atio n , the PC hlide and M g-P roto IX portions o f the difference spectrum were reduced an d the P roto IX peak an d peak n ear 503 nm were increased. D Y treatm en t yielded a difference spectrum w ith peaks approxim ating those o f Proto IX an d M g-Proto IX M E , along w ith a peak n ear 503 nm . T he presence o f all porp h y rin s detected by in vivo sp ectro p h o to m etry except fo r the 503 nm p eak w as confirm ed w ith H PL C . Proto IX m onom ethyl ester was found by H P L C to be espe cially elevated in treatm ents with AF. The in vivo 503 nm peak a n d in vitro studies w ith Protoxco n tain in g barley etioplast p reparations suggest th a t p ro to te tra h y d ro p o rp h y rin IX (an oxid a tion state interm ediate between proto p o rp h y rin o g en IX an d P roto IX ) m ay accum ulate un d er som e conditions. These d ata dem onstrate th at rapid in vivo spectro p h o to m etric studies can provide m uch o f the qualitative results o f H P L C studies and can confirm th a t in vitro results co rresp o n d with the in vivo situation.

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Catabolite repression of protoporphyrin IX biosynthesis in Escherichia coli K‐12

Cited by 19 publications

References 10 publications

Characterization of the oxygen-dependent promoter of the Vitreoscilla hemoglobin gene in Escherichia coli

Characterization of the oxygen-dependent promoter of the Vitreoscilla hemoglobin gene in Escherichia coli

Hemes, Chlorophylls, and Related Compounds: Biosynthesis and Metabolic Regulation

HPLC and in vivo Spectrophotometric Detection of Porphyrins in Plant Tissues Treated with Porphyrinogenic Herbicides

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