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Selected Works

1994

Molecular Biology

Articles 1 - 3 of 3

Full-Text Articles in Life Sciences

Molecular Genetic Analysis Of Terminal Steps In Bacteriochlorophyll A Biosynthesis: Characterization Of A Rhodobacter Capsulatus Strain That Synthesizes Geranylgeranoil-Esterified Bacteriochlorophyll A, David Bollivar, Shaojie Wang, James P. Allen, Carl E. Bauer Oct 1994

Molecular Genetic Analysis Of Terminal Steps In Bacteriochlorophyll A Biosynthesis: Characterization Of A Rhodobacter Capsulatus Strain That Synthesizes Geranylgeranoil-Esterified Bacteriochlorophyll A, David Bollivar, Shaojie Wang, James P. Allen, Carl E. Bauer

David Bollivar

Site-directed mutational analysis of the Rhodobacter capsulatus photosynthesis gene cluster was undertaken in order to identify and characterize genetic loci involved in bacteriochlorophyll a biosynthesis. A mutant in orf304 was shown to accumulate the tetrapyrrole intermediate "bacteriochlorophyllide a" which is a tetrapyrrole that has a bacteriochlorophyll a ring structure without the presence of an esterifying alcohol. A mutant in orf391 is shown to synthesize acteriochlorophyll a that is esterified with geranylgeraniol rather than the normal phytol. This latter result provides the first genetic confirmation that esterification of bacteriochlorophyllide a initially involves the addition of a geranylgeraniol group followed by sequential …


Heterologous Expression Of The Bchm Gene Product From Rhodobacter Capsulatus And Demonstration That It Encodes S-Adenosyl-L-Methionine: Mg-Protoporhyrin Ix Methyltransferase, David Bollivar, Ze-Yu Jiang, Carl E. Bauer, Samuel I. Beale Aug 1994

Heterologous Expression Of The Bchm Gene Product From Rhodobacter Capsulatus And Demonstration That It Encodes S-Adenosyl-L-Methionine: Mg-Protoporhyrin Ix Methyltransferase, David Bollivar, Ze-Yu Jiang, Carl E. Bauer, Samuel I. Beale

David Bollivar

The bacteriochlorophyll biosynthesis gene, bchM, from Rlodobacter capsulatus was previously believed to code for a polypeptide involved in formation of the cyclopentone ring of protochlorophyllide from Mg-protoporphyrin IX monomethyl ester. In this study, R. capsulatus bchM was expressed in Escherichia coli and the gene product was subsequently demonstrated by enzymatic analysis to catalyze methylation of Mg-protoporphyrin IX to form Mg-protoporphyrin IX monomethyl ester. Activity required the substrates Mg-protoporphyrin IX and S-adenosyl-L-methionine. 14C-labeled product was formed in incubations containing 14C-methyl-labeled S-adenosyl-L-methionine. On the basis of these and previous results, we also conclude that the bchH gene, which was previously reported to …


Altering The Rna Binding Specificity Of A Translational Repressor, F Lim, Marc Spingola, D S. Peabody Mar 1994

Altering The Rna Binding Specificity Of A Translational Repressor, F Lim, Marc Spingola, D S. Peabody

Marc Spingola

The coat proteins of RNA phages MS2 and GA are specific RNA-binding proteins which function to encapsidate viral RNA and to translationally repress synthesis of the viral replicase. The two proteins have highly homologous amino acid sequences, yet they show different RNA binding specificities, recognizing RNA stem-loop structures which differ primarily in the nucleotide sequences of their loops. We sought to convert MS2 coat protein to the RNA binding specificity of GA through the introduction of GA-like amino acid substitutions into the MS2 coat protein RNA-binding site. The effects of the mutations were determined by measuring the affinity of the …