Regions of variant histone His2AvD required for Drosophila development
It is shown that the unique feature of His2AvD does not reside in its histone fold but in its carboxy-terminal domain, which maps to a short α-helix in H2A that is buried deep inside the nucleosome core.
THE BIOSYNTHESIS OF PHENYLALANINE AND TYROSINE; ENZYMES CONVERTING CHORISMIC ACID INTO PREPHENIC ACID AND THEIR RELATIONSHIPS TO PREPHENATE DEHYDRATASE AND PREPHENATE DEHYDROGENASE.
The isolation and characterization of a hydroxamic acid (aerobactin) formed by Aerobacter aerogenes 62-1
Membrane-associated reactions in ubiquinone biosynthesis in Escherichia coli. 3-Octaprenyl-4-hydroxybenzoate carboxy-lyase.
Oxidative phosphorylation in Escherichia coli K12. Mutations affecting magnesium ion- or calcium ion-stimulated adenosine triphosphatase.
Determination of the Mg(2+,Ca(2+)-stimulated adenosine triphosphatase activities in the mutant and normal strains indicated that the uncA gene is probably the structural gene for Mg (2+),Ca( 2+)- Stimulated adenoine tri phosphatase, which appears to be essential for oxidative phosphorylation in E. coli.
Biosynthesis of Ubiquinone in Escherichia coli K-12: Location of Genes Affecting the Metabolism of 3-Octaprenyl-4-hydroxybenzoic Acid and 2-Octaprenylphenol
Two genes (ubiB and ubiD) concerned with two successive reactions in ubiquinone biosynthesis in Escherichia coli were mapped and found to be closely linked. Mutant strains of E. coli carrying the…
Mutations affecting the cytochrome d-containing oxidase complex of Escherichia coli K12: identification and mapping of a fourth locus, cydD.
A mutant of Escherichia coli K12 has been isolated affected in a gene, designated cydD, distinct from the three previously described loci involved in the synthesis of assembly of the cytochrome bd oxidase complex, consistent with cotransduction frequencies.
The structure of enterochelin and related 2,3-dihydroxy-N-benzoylserine conjugates from Escherichia coli.
Enterochelin hydrolysis and iron metabolism in Escherichia coli.
The cydD gene product, component of a heterodimeric ABC transporter, is required for assembly of periplasmic cytochrome c and of cytochrome bd in Escherichia coli.
It is demonstrated that a cydD mutant also fails to synthesise periplasmic c-type cytochrome(s), suggesting that the transporter exports haem or some other component involved in assembly of cytochromes that are found in, or exposed to, the periplasms.