Protein targeting: Getting into the groove

Current Biology

Volumn 8, Issue 20, 1998, Pages

  Bernstein, Harris D ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0032497570     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/s0960-9822(98)70456-7     Document Type: Article

References (23)

1. Walter P, Johnson AE: Signal sequence recognition and protein targeting to the endoplasmic reticulum. Annu Rev Cell Biol 1994, 10:87-119.
2. Kaiser CA, Preuss D, Grisafi P, Botstein D: Many random sequences functionally replace the secretion signal sequence of yeast invertase. Science 1987, 235:312-317.
3. Römisch K, Webb J, Lingelbach K, Gausepohl H, Dobberstein B: The 54-kD protein of signal recognition particle contains a methionine-rich RNA binding domain. J Cell Biol 1990, 111:1793-1802.
4. Zopf D, Bernstein HD, Johnson AE, Walter P: The methionine-rich domain of the 54-kD protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence. EMBO J 1990, 9:4511-4517.
5. Bernstein HD, Poritz MA, Strub K, Hoben PJ, Brenner S, Walter P: Model for signal sequence recognition from amino-acid sequence of 54 kDa subunit of signal recognition particle. Nature 1989, 340:482-486.
6. Gellman S: On the role of methionine residues in the sequence-independent recognition of nonpolar protein surfaces. Biochemistry 1991, 30:6633-6636.
7. Ikura M, Clore GM, Gronenborn AM, Zhu G, Klee CB, Bax A: Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 1992, 256:632-638.
8. Meador WE, Means AR, Quiocho FA: Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex. Science 1992, 257:1251-1255.
9. Chen Q, Vierling E: Analysis of conserved domains identifies a unique structural feature of a chloroplast heat shock protein. Mol Gen Genet 1991, 226:425-431.
10. Keenan RJ, Freymann DM, Walter P, Stroud RM: Crystal structure of the signal sequence binding subunit of the signal recognition particle. Cell 1998, 94:181-191.
11. McKnight CJ, Briggs MS, Gierasch LM: Functional and nonfunctional LamB signal sequences can be distinguished by their biophysical properties. J Biol Chem 1989, 264:17293-17297.
12. Zheng N, Gierasch LM: Domain interactions in E. coli SRP: Stabilization of M domain by RNA is required for effective signal sequence modulation of NG domain. Mol Cell 1997, 1:79-87.
13. Kurita K, Honda K, Suzuma S, Takamatsu H, Nakamura K, Yamane K: Identification of a region of Bacillus subtilis Ffh, a homologue of mammalian SRP54 protein, that is essential for binding to small cytoplasmic RNA. J Biol Chem 1996, 271:13140-13146.
14. Zopf D, Bernstein HD, Walter P: GTPase domain of the 54-kD subunit of mammalian signal recognition particle is required for protein translocation but not for signal sequence binding. J Cell Biol 1993, 120:1113-1121.
15. Newitt JA, Bernstein HD: The N-domain of the signal recogntion particle 54-kDa subunit promotes efficient signal sequence binding. Eur J Biochem 1997, 245:720-729.
16. Miller JD, Wilhelm H, Gierasch L, Gilmore R, Walter P: GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation. Nature 1993, 366:351-354.
17. Walter P, Ibrahimi I, Blobel G: Translocation of proteins across the endoplasmic reticulum. I. Signal recogntion protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein. J Cell Biol 1981, 91:545-550.
18. Beckmann R, Bubeck D, Grassucci R, Penczek P, Verschoor A, Blobel G, Frank J: Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex. Science 1997, 278:2123-2126.
19. Rapiejko PJ, Gilmore R: Empty site forms of the SRP54 and SRa GTPases mediate targeting of ribosome-nascent chain complexes to the endoplasmic reticulum. Cell 1997, 89:703-713.
20. Freymann DM, Keenan RJ, Stroud RM, Walter P: Structure of the conserved GTPase domain of the signal recognition particle. Nature 1997, 385:361-364.
21. Montoya G, Svensson C, Luirink J, Sinning I: Crystal structure of the NG-domain from the signal recognition particle receptor FtsY. Nature 1997, 385:365-368.
22. de Gier JW, Mansournia P, Valent QA, Phillips GJ, Luirink J, von Heijne G: Assembly of a cytoplasmic membrane protein is dependent on the signal recognition particle. FEBS Lett 1996, 399:307-309.
23. Ulbrandt ND, Newitt JA, Bernstein HD: The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins. Cell 1997, 88:187-196.