Association of the Halobacterial 7S RNA to the Polysome Correlates with Expression of the Membrane Protein Bacterioopsin

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 89; no. 4; pp. 1204 - 1208
• Main Authors: Gropp, Roswitha, Gropp, Felix, Betlach, Mary C.
• Format: Journal Article
• Language: English
• Published: Washington, DC National Academy of Sciences of the United States of America 15.02.1992; National Acad Sciences; National Academy of Sciences
• Subjects: Amino Acid Sequence; Amino acids; Analytical, structural and metabolic biochemistry; Bacteria; Bacteriorhodopsins - metabolism; Biochemistry; Biological and medical sciences; Cell growth; Fundamental and applied biological sciences. Psychology; Gels; Halobacterium - metabolism; Membrane Glycoproteins - chemistry; Membrane Glycoproteins - metabolism; Membrane proteins; Membrane Proteins - chemistry; Membrane Proteins - metabolism; Messenger RNA; Molecular Sequence Data; Nucleic acids; P branes; Polyribosomes; Polyribosomes - metabolism; Proteins; Puromycin - pharmacology; Ribonucleic acid; Ribonucleoproteins - metabolism; Ribosomes; Ribosomes - metabolism; RNA; RNA, Messenger - metabolism; Rna, ribonucleoproteins; RNA, Ribosomal, 5S - metabolism; RNA, Small Nuclear - metabolism; Signal Recognition Particle; Ultracentrifugation; Membrane protein; Ribonucleoprotein; Archaeobacteria; Genetical translation; Photoprotein; Halobacterium halobium; Bacteriorhodopsin; Messenger RNA; Apoproteins; Molecular association; Bacteria; Halobacteriaceae; Polysome
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.89.4.1204

The sedimentation behavior of the halobacterial 7S RNA and bacterioopsin mRNA was assessed after application of total cell lysates to sucrose gradients. These two RNAs cosedimented predominantly with membrane-bound polysomes, and the quantity of 7S RNA bound to the ribosomes was directly correlated with the expression of bacterioopsin. Puromycin treatment released the 7S RNA from the polysomes, indicating that it is transiently associated with protein translation. We suggest that halobacteria contain a signal-recognition-like particle involved in translation of membrane-associated proteins.