Putative integral membrane SRP receptors [1]

Trends in Biochemical Sciences

Volumn 26, Issue 1, 2001, Pages 15-16

  Bibi, Eitan ^a   Herskovits, Anat A ^a   Bochkareva, Elena S ^a   Zelazny, Adrian ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

DOCKING PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; SIGNAL RECOGNITION PARTICLE;

ENDOPLASMIC RETICULUM; ESCHERICHIA COLI; HYBRID; HYDROPHOBICITY; LETTER; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN TARGETING; RECEPTOR BINDING; RECEPTOR UPREGULATION; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION; STRAIN DIFFERENCE;

ESCHERICHIA COLI;

EID: 85041133083     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(00)01711-4     Document Type: Letter

References (12)

1. New prospects in studying the bacterial signal recognition particle pathway
2. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
3. The NG domain of the prokaryotic signal recognition particle receptor, FtsY, is fully functional when fused to an unrelated integral membrane polypeptide
4. Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor
5. An alternative protein targeting pathway in Escherichia coli: Studies on the role of FtsY
6. Membrane association of FtsY, the E. coli SRP receptor
7. Anionic phospholipids are involved in membrane association of FtsY and stimulate its GTPase activity
8. A site-specific, membrane-dependent cleavage event defines the membrane binding domain of FtsY
9. SRPDB (signal recognition particle database)
10. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
11. The signal recognition particle receptor α subunit assembles co-translationally on the endoplasmic reticulum membrane during an mRNA-encoded translation pause in vitro
12. A simple method for displaying the hydropathic character of a protein