Expression, crystallization and preliminary x-ray diffraction study of FtsY, the docking protein of the signal recognition particle of E. coli

Proteins: Structure, Function and Genetics

Volumn 28, Issue 2, 1997, Pages 285-288

  Montoya, Guillermo ^a   Svensson, Cecilia ^a   Luirink, Joen ^b   Sinning, Irmgard ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b Biocentrum Amsterdam   (Netherlands)

Author keywords

Crystallization; Expression; GTPase; SRP; SRP receptor; X ray diffraction

Indexed keywords

DOCKING PROTEIN; GUANOSINE TRIPHOSPHATE; SECRETORY PROTEIN; SIGNAL RECOGNITION PARTICLE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE; CRYSTALLIZATION; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN TARGETING; SYNCHROTRON; X RAY DIFFRACTION;

BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; RECEPTORS, CYTOPLASMIC AND NUCLEAR; RECOMBINANT PROTEINS; SIGNAL RECOGNITION PARTICLE;

ESCHERICHIA COLI;

EID: 0030910803     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199706)28:2<285::AID-PROT15>3.0.CO;2-E     Document Type: Article

References (20)

1. Luirink, J., Dobberstein, B. Mammalian and E. coli signal recognition particles. Mol. Microbiol. 11:1-9, 1994.
2. Lütcke, H. Signal recognition particle (SRP), a ubiquitous initiator of protein translocation. Eur. J. Biochem. 228:531-550, 1995.
3. Siegel, V., Walter, P. Each of the activities of signal recognition particle (SRP) is contained within a distinct domain: analysis of biochemical mutants of SRP. Cell 52:39-49, 1988.
4. Conolly, T., Gilmore, R. The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide Cell 57:599-610, 1989.
5. Miller, J.D., Tajima, S., Lauffer, L., Walter, P. The β subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the α subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membrane. J. Cell Biol. 128:273-282, 1995.
6. Pugsley, A.P. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57:50-108, 1993.
7. Poritz, S., Bernstein, H.D., Strub, K., Zopf, D., Wilhelm, H., Walter, P. An E. coli ribunucleoprotein containing 4.5S RNA resembles mammalian signal recognition particle. Science 250:1111-1117, 1990.
8. Ribes, V., Roemisch, K., Giner, A., Dobberstein, B., Tollervey, D. E. coli 4.5S RNA is part of a ribonucleoprotein particle that has properties related to signal recognition particle. Cell 63:591-600, 1990.
9. Römisch, K., Webb, J., Herz, J., Prehn, S., Frank, R., Vingeron, M., Dobberstein, B. Homology of 54K protein of signal recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains. Nature 340: 478-482, 1989.
10. Bernstein, H.D., Poritz, M.A., Strub, K., Hoben, P.J., Brenner, S., Walter, P. Model for signal sequence recognition from amino acid sequence of 54K subunit of signal recognition particle. Nature 340:482-486, 1989.
11. Luirink, J., ten Hagen-Jongman, C., van der Weijden, C. C., Oudega, B., High, S., Dobberstein, B., Kusters, R. An alternative protein targeting pathway in E. coli: studies on the role of FtsY. EMBO J. 13:2289-2296, 1994.
12. Miller, J.D., Bernstein, H.D., Walter, P. Interaction of E. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor Nature 367:657-659, 1994.
13. Powers, T., Walter, P. Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases. Science 269:1422-1424, 1995.
14. Gill, D.R., Salmond, G.P.C. The identification of the Escherichia coli ftsY gene product: an unusual protein. Mol. Miocrobiol. 4:575-583, 1990.
15. Bourne, H.R., Sanders, D.A., McCormick, F. The GTPase superfamily: Conserved structure and molecular mechanism. Nature 349:117-127, 1991.
16. John, J., Sohmen, R., Feuerstein, J., Linke, R., Wittinghofer, A., Goody, R.S. Kinetics of interaction of nucleotides with nucleotide-free H-ras p21. Biochemistry 29:6058-6065, 1990.
17. Otwinowski, Z., Data collection and processing. In: "Proceedings of the CCP4 Study Weekend." Warrington, UK: Daresbury Laboratory. 1993:56-62.
18. Kusters, R., Lentzen, G., Eppens, E., van Geel, A., van der Weijden, C.C., Wintermeyer, W., Luirink, J. The functioning of the SRP receptor FtsY in protein-targeting in E. coli is correlated with its ability to bind and hydrolyse GTP. FEES Lett. 372:253-258, 1995.
19. Matthews, B.W. Solvent content of protein crystals. J. Mol. Biol. 33:491-497, 1968.
20. Hendrickson, W.A. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation Science 254:51-58, 1991.