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Biomedical subjects

B F Clark

Publications and source records attributed to B F Clark.

At least 127 records · Page 7Linked to original sources
PubMed1980

Primary structure of elongation factor Tu from Escherichia coli.

The amino acid sequence of elongation factor Tu (EF-Tu) from Escherichia coli has been determined. EF-Tu is a single-chain polypeptide composed of 393 amino acids (Mr 43,225 for the species bearing COOH-terminal serine). The NH2-terminal serine is acetylated, and lysine-56 is partially methylated. The sites of facile tryptic cleavage are at arginines 44 and 58 and at lysine-263. The cysteinyl residues associated with aminoacyl-tRNA and guanosine nucleotide binding activities are residues 81 and 137, respectively. The COOH-terminal amino acid is heterogenous in that analyses of the COOH-terminal peptides isolated from different EF-Tu preparations gave position 393 as glycine and serine in ratios (Gly/Ser) ranging from about 0.7 to 3.

Amino Acid Sequence↗
PubMed1980

The effect of chemical modification of the CCA end of yeast tRNAPhe on its biological activity on ribosomes.

Yeast tRNAPhe containing 2-thiocytidine (s2C) at position 75 was alkylated specifically at this residue. The biological activities of alkylated and native tRNAPhe were compared in an Escherichia coli protein-synthesizing system in vitro. The alkylated tRNAPhe proved to be active in all steps involved in the elongation phase but the rate of the peptide transfer reaction was somewhat lower when the alkylated tRNAPhe acted as an acceptor of peptidyl residues as compared to native tRNAPhe. These results raise the possibility for attaching spectroscopic or affinity labels at the s2C-75 residue of tRNAPhe without impairing the activity of the tRNA.

Base Sequence↗
PubMed1980

The complete amino-acid sequence of elongation factor Tu from Escherichia coli.

The complete primary structure of elongation factor Tu from Escherichia coli has been elucidated. The protein, which is a mixture of two gene products, consists of a single polypeptide chain of 393 residues. After tryptic digestion of S-carboxymethylated protein, 50 tryptic peptides were isolated covering the complete protein chain. Their alignment was established with overlapping peptides obtained by chemical cleavage with cyanogen bromide and subsequent enzymic subdigestion with Staphylococcus aureus protease, chymotrypsin, elastase and thermolysin. Peptides were sequenced by manual dansyl-Edman and direct Edman degradation procedures. The N-terminal amino acid of EF-Tu is serine and is N-acetylated. The lysine residue at positon 56, in the polypeptide chain is partly methylated. The C-terminal residue is a mixture of serine and glycine, and this was the only heterogeneity found in the EF-Tu preparation used in this study.

Amino Acid Sequence↗
PubMed1980

Absence of oestradiol-17 beta dehydrogenase from the progesterone-dominated mouse uterus.

In the mouse uterus the development of sensitivity to a decidualizing stimulus requires large amounts of progesterone and small amounts of oestradiol-17 beta. During the process progesterone induces changes in the sensitivity of the tissues of the uterus to oestrogen. From observations of human endometrium it has been suggested that progesterone modulates the biological activity of oestradiol-17 beta by stimulating the metabolic conversion of oestradiol-17 beta to oestrone. Accordingly [6,7-3H]oestradiol-17 beta was injected subcutaneously into ovariectomized mice at various stages of the development of sensitivity to a decidualizing injection of oil into the uterine lumen. Radioactivity was extracted 4 h later, fractionated and identified. There was no alteration in the amounts of oestradiol, oestrone or water-soluble metabolites in the uteri whether the mice were treated with progesterone or with progesterone plus oestrogen or whether the uterine horns were decidualized for 24 or 48 h. The results suggest that in vivo the metabolism of oestradiol-17 beta by the uterus is not stimulated by progesterone.

17-Hydroxysteroid Dehydrogenases↗
PubMed1978

The effect of specific structural modification on the biological activity of E. coli arginine tRNA.

Escherichia coli arginine tRNA1 has been modified at position s2C32 with iodoacetamide and a spin labelled derivative. The small effects on the charging ability of tRNA by the modifiications suggest that the synthetase does not bind to the tRNA in this region of the anticodon loop before the anticodon. A ternary complex of elongation factor Tu, GTP and the modified Arg-tRNA, can be formed allowing future studies of enzymatic binding to the ribosome. Using the triplet binding assay the native Arg-tRNA1 decodes all 4 codons beginning with CG. The modified Arg-tRNA1 has a restricted decoding but the decoding pattern is still unusual according to the Wobble Hypothesis.

Amino Acyl-tRNA Synthetases↗
PubMed1975

Structure of yeast phenylalanine transfer RNA at 2.5 A resolution.

The x-ray analysis of the monoclinic form of yeast tRNAPhe has been taken to a resolution of 2.5 A by the method of isomorphous replacement. The model proposed at 3 A has been confirmed and extended to reveal additional features of the tertiary structure and of the stereochemistry. An extensive hydrogen bonding network is described involving specific interactions between bases and the ribose-phosphate backbone. The structure of a G-U base pair has been solved.

Base Sequence↗
PubMed1974

The selective reaction of methoxyamine with cytidine residues in mammalian initiator transfer ribonucleic acid.

Methoxyamine reacts selectively with tRNA molecules at certain exposed cytosine residues usually located in non base-paired regions of the two dimensional clover leaf structure. Here methoxyamine is used for the first time in a study of a mammalian tRNA structure. One of the sequence abnormalities of myeloma initiator tRNA is a cytosine instead of the usual uracil immediately preceding the anticodon. A study of the reaction of the cytosine residues with methoxyamine indicates that the accessibility of bases to chemical reagents in the anticodon loop of this mammalian initiator tRNA is very similar to that observed for the bacterial initiator tRNA.

Animals↗