Isolation and characterization of visible light-sensitive mutants of Escherichia coli K12

Miyamoto, Kazuhito; Nakahigashi, Kenji; Nishimura, Koichi; Inokuchi, Hachiro

doi:10.1016/0022-2836(91)90180-e

Cited by 99 publications

(71 citation statements)

References 16 publications

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“…The mitochondrial fraction and 0.05 M sodium phosphate buffer (pH 7.3) containing 0.05 M malate were incubated at 25°C, and the amount of the reaction product, fumarate, was determined by measuring the absorbance at 250 nm. 2 Cleary, S. M., Tan, F.-C., Nakrieko, K.-A., Thompson, S. J., Mullineaux, P. M., Creissen, G. P., von Stedingk, E., Glaser, E., Smith Electrophoresis of Partially Denatured Thylakoid-Chlorophyll-protein complexes were separated as described by Andersson et al (24), with slight modifications. Thylakoids equivalent to 50 g of chlorophyll were solubilized at 4°C in 100 l of 0.3 M Tris-HCl, pH 8.8, 13% glycerol, and SDS (0.4%, 1%, or 2%).…”

Section: Construction Of Gstmentioning

confidence: 99%

“…It has recently been demonstrated that the mitochondrial import system in vitro is not robust because it will readily import a number of precursors that are found exclusively in the chloroplast in vivo. 2 Therefore, it is not possible to extrapolate the location of a protein in vivo from the results of a mitochondrial import experiment. Nevertheless, it was a useful test to discriminate between the two classes of ferrochelatase.…”

Section: Import In Vitro Of Csfec Precursors Into Isolated Pea Organementioning

confidence: 99%

“…In yeast and mammalian mitochondria, ferrochelatase is associated with inner mitochondrial membranes as the mature form of a higher molecular weight precursor (1). Ferrochelatases have been purified from bacteria, yeast, and mammals, and many cDNAs have been isolated (2)(3)(4)(5). In each case, only one type of ferrochelatase has been isolated.…”

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confidence: 99%

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Two Types of Ferrochelatase in Photosynthetic and Nonphotosynthetic Tissues of Cucumber

Suzuki¹,

Masuda²,

Singh³

et al. 2002

Journal of Biological Chemistry

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Ferrochelatase catalyzes the insertion of Fe2؉ into protoporphyrin IX to generate protoheme. In higher plants, there is evidence for two isoforms of this enzyme that fulfill different roles. Here, we describe the isolation of a second ferrochelatase cDNA from cucumber (CsFeC2) that was less similar to a previously isolated isoform (CsFeC1) than it was to some ferrochelatases from other higher plants. In in vitro import experiments, the two cucumber isoforms showed characteristics similar to their respective ferrochelatase counterparts of Arabidopsis thaliana. The C-terminal region of CsFeC2 but not CsFeC1 contained a conserved motif found in light-harvesting chlorophyll proteins, and CsFeC2 belonged to a phylogenetic group of plant ferrochelatases containing this conserved motif. We demonstrate that CsFeC2 was localized predominantly in thylakoid membranes as an intrinsic protein, and forming complexes probably with the C-terminal conserved motif, but a minor portion was also detected in envelope membranes. CsFeC2 mRNA was detected in all tissues and was light-responsive in cotyledons, whereas CsFeC1 mRNA was detected in nonphotosynthetic tissues and was not light-responsive. Interestingly, tissue-, light-, and cycloheximide-dependent expressions of the two isoforms of ferrochelatase were similar to those of two glutamyl-tRNA reductase isoforms involved in the early step of tetrapyrrole biosynthesis, suggesting the existence of distinctly controlled tetrapyrrole biosynthetic pathways in photosynthetic and nonphotosynthetic tissues.

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Section: Construction Of Gstmentioning

confidence: 99%

Section: Import In Vitro Of Csfec Precursors Into Isolated Pea Organementioning

confidence: 99%

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Two Types of Ferrochelatase in Photosynthetic and Nonphotosynthetic Tissues of Cucumber

Suzuki¹,

Masuda²,

Singh³

et al. 2002

Journal of Biological Chemistry

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“…Two separate regions of Orf9 show similarity to E. coli ferrochetalase (42.5% identity over 20% of the complete Orf9 sequence). Ferrochetalase is the final enzyme in the biosynthesis of heme, catalyzing the chelation of ferrous iron into the tetrapyrrole ring of protoporphyrin IX (Miyamoto et al, 1991). Interestingly, protoporphyrin 1X appears to be the photosensitizer for the light-induced synthesis of carotenoids in M. xanthus (Burchard and Hendricks, 1969).…”

Section: Sequence Relationship Of Orf5 To Neurosporene Hydratasementioning

confidence: 99%

A Cluster of Structural and Regulatory Genes for Light‐Induced Carotenogenesis in Myxococcus xanthus

Botella

Murillo

Ruiz‐Vázquez

1995

European Journal of Biochemistry

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In the bacterium Myxococcus xanthus, several genes for carotenoid synthesis lie together at the carAcarB chromosomal locus and are co-ordinately activated by blue light. A 12-kb DNA stretch from wildtype M. xanthus has been sequenced that includes the entire carA-carB gene cluster. According to sequence analysis, the cluster contains 11 different genes. Intergenic distances are very short or nil (implying translational coupling), giving further support to previous evidence indicating that most (or all) of the genes in the cluster form a single operon. At the promoter region, a potential -35 site for the binding of ~7 factors is found. However, the -10 region shows little similarity with analogous sites in other bacterial promoters. Five (possibly six) genes in the curA-curB operon code for enzymes acting on early or late steps of the pathway for carotenoid synthesis. Other genes in the operon show no overall similarity with previously known genes. However, peptide stretches in the predicted products of two genes exhibit strong similarity with the DNA binding domain of the MerR family of transcriptional regulators. At least one of the predicted DNA-binding domains is altered in a mutant strain affected in light-regulation of the car genes.

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“…Gene for Escherichia coli ferrochelatase was characterized, and the open reading frame encoded 320 amino acid residues (Miyamoto et al 1991). Deduced amino acid sequence of the bacterial enzyme shows 26-28% identities to those of the mammalian enzymes.…”

Section: Location Of Ferrochelatase In Mitochondriamentioning

confidence: 99%

Molecular and Genetic Characterization of Ferrochelatase.

Taketani

1993

Tohoku J. Exp. Med.

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Isolation and characterization of visible light-sensitive mutants of Escherichia coli K12

Cited by 99 publications

References 16 publications

Two Types of Ferrochelatase in Photosynthetic and Nonphotosynthetic Tissues of Cucumber

Two Types of Ferrochelatase in Photosynthetic and Nonphotosynthetic Tissues of Cucumber

A Cluster of Structural and Regulatory Genes for Light‐Induced Carotenogenesis in Myxococcus xanthus

Molecular and Genetic Characterization of Ferrochelatase.

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