Identification of a bacterio‐opsin species with a N‐terminally extended amino acid sequence

Dellweg, Hansgeorg; Sumper, Manfred

doi:10.1016/0014-5793(80)80668-5

Cited by 16 publications

(5 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Gene sequencing (Dunn et al, 1981) and mRNA translation (Dellweg & Sumper, 1980) both indicate that bR possesses a N-terminal leader peptide, albeit one of unique structure. The supposition is that it serves a similar function to the eukaryotic signal peptides of nascent secretory proteins (for review see Sabatini et al, 1982).…”

Section: Biosynthesismentioning

confidence: 99%

The opsin family of proteins

Findlay¹,

Pappin²

1986

Biochemical Journal

249

102

View full text Add to dashboard Cite

Section: Biosynthesismentioning

confidence: 99%

The opsin family of proteins

Findlay¹,

Pappin²

1986

Biochemical Journal

249

102

View full text Add to dashboard Cite

“…In this report, we demonstrate that the halobacterial 7S RNA is associated with ribosomes during translation, and our data suggest that it is specifically involved in translation of membrane proteins. (18,19). The precursor is processed in a two-step mechanism (20, 21), but processing is not necessary for correct folding of the protein.…”

Section: Introductionmentioning

confidence: 99%

“…(17). Bacterioopsin is synthesized as a precursor with 13 extra N-terminal amino acids (18,19). The precursor is processed in a two-step mechanism (20,21), but processing is not necessary for correct folding of the protein.…”

mentioning

confidence: 99%

Association of the halobacterial 7S RNA to the polysome correlates with expression of the membrane protein bacterioopsin.

Gropp

Betlach

1992

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The sedimentation behavior of the halobacterial 7S RNA and bacterioopsin mRNA was ass 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 signalrecognition-like particle involved in translation of membraneassociated proteins.In mammalian cells the 7S RNA is part of the signal recognition particle (SRP), which mediates cotranslational processing mechanisms for membrane and secretory proteins (1,2). SRP is a ribonucleoparticle that recognizes the leader sequence ofthe nascent polypeptide chain as it emerges from the ribosome. The interaction causes a translational arrest that is only released if the complex is targeted to a receptor in the membrane (3). These mechanisms prevent synthesis of hydrophobic proteins in a hydrophilic environment and direct membrane and secretory proteins to their final destinations in the cell. Small ribonucleoproteins resembling SRP have also been found in yeast (Schizosaccharomyces pombe and Yarrowia lipolytica) and in Escherichia coli (4-6), but in contrast to mammalian cells they translocate many proteins posttranslationally; genetic studies do not as yet corroborate a SRP-coupled translocation mechanism (7-9). Genetic analysis in E. coli has shown that the 4.5S RNA, which has been identified as a component of the ribonucleoparticle, is acting on translating ribosomes and perhaps in concert with elongation factor G GTP (10). However, it remains unclear whether it is generally obligatory for translation or only participates in translation of a subset of proteins.Like other archaebacteria, Halobacterium halobium possesses a 7S RNA with a possible secondary structure almost identical to that of the mammalian SRP RNA (11-13). Its function is unknown, but as archaebacterial 7S RNA genes can replace the 4.5S RNA gene in E. coli (14), it is likely that a signal recognition-like particle exists in halobacteria. In this report, we demonstrate that the halobacterial 7S RNA is associated with ribosomes during translation, and our data suggest that it is specifically involved in translation of membrane proteins. (18,19). The precursor is processed in a two-step mechanism (20, 21), but processing is not necessary for correct folding of the protein. Both forms integrate into the-purple membrane with no conformational differences from the mature protein (22). The presequence is unusual and lacks similarities to other prokaryotic and eukaryotic signal sequences (23). This observation raises questions about its functional significance. In this report we show that the N-terminal sequences of six halobacterial integral membrane proteins share a common motif that may be of functional importance. MATERIALS AND METHODSRNAzol was purchase...

show abstract

“…the archaebacteria. Several genes coding for integral membrane proteins or for secreted proteins have been found to code for signal sequences similar to those found in eukaryotes and eubacteria (Dellweg and Sumper, 1980;Dunn et ai, 1981;Lechner and Sumper. 1987;Lin and Tang, 1990).…”

Section: Introductionmentioning

confidence: 91%

A gene in the archaebacterium Sulfolobus solfataricus that codes for a protein equivalent to the alpha subunits of the signal recognition particle receptor in eukaryotes

Ramı́rez

Matheson

1991

Molecular Microbiology

View full text Add to dashboard Cite

We have sequenced a gene in the archaebacterium Sulfolobus solfataricus that codes for a protein that shows sequence similarity to the alpha subunit of the signal recognition particle receptor or docking protein in eukaryotes and the product of the ftsY gene in Escherichia coli. Comparison of the Sulfolobus 'docking protein' with its eukaryotic and eubacterial counterparts showed that the region of highest sequence similarity corresponds to a GTP-binding site. The presence of this gene in archaebacteria suggests that some of the components involved in protein transport have been conserved in the three kingdoms.

show abstract

Identification of a bacterio‐opsin species with a N‐terminally extended amino acid sequence

Cited by 16 publications

References 18 publications

The opsin family of proteins

The opsin family of proteins

Association of the halobacterial 7S RNA to the polysome correlates with expression of the membrane protein bacterioopsin.

A gene in the archaebacterium Sulfolobus solfataricus that codes for a protein equivalent to the alpha subunits of the signal recognition particle receptor in eukaryotes

Contact Info

Product

Resources

About