PubMed Health⌕ Search

Biomedical subjects

F A Jay

Publications and source records attributed to F A Jay.

3 recordsLinked to original sources

The orientation of halorhodopsin in the cell membrane of halobacteria.

The orientation of the light-driven chloride pump, halorhodopsin, in the membrane was determined using antibodies directed against a synthetic peptide which represents the C-terminal segment of the protein. Antibodies against this decapeptide did not bind to right-side-out cell vesicles. Partial inversion by sonication or lysis under low salt conditions exposed this COOH-terminal antigenic site. Antibody binding was removed by preincubation with the decapeptide. The COOH terminus of the molecule is therefore located on the cytoplasmic surface of the membrane.

Amino Acid Sequence↗

Reversible chemical cross-linking of the light-harvesting polypeptides of Rhodopseudomonas viridis.

The topography of the light-harvesting polypeptides of Rhodopseudomonas viridis was investigated using cleavable chemical cross-linkers. To this end a set of succinimidyl esters and surface-specific sulfosuccinimidyl esters of different span widths were synthesized. The cross-linking reagents have been characterized using NMR and infrared spectroscopy and thin-layer chromatography. The cross-linking reaction was carried out under physiological conditions and the aggregates were analyzed by the methods of one- and two-dimensional polyacrylamide gel electrophoresis and by immunoblot analysis. We found cross-linkage between B1015-alpha and B1015-alpha, between B1015-alpha and B1015-beta and B1015-beta and B1015-beta. Aggregates of higher molecular mass were hetero-oligomers of B1015-alpha and B1015-beta containing three and four polypeptides, respectively. The results obtained in this work indicate a very tight contact among the light-harvesting polypeptides. We assume that the light-harvesting polypeptides are localized alternately as dimers of B1015-alpha and B1015-beta around the reaction centre core.

Bacterial Proteins↗