Structure and function of a membrane component SecDF that enhances protein export

Nature

Volumn 474, Issue 7350, 2011, Pages 235-238

  Tsukazaki, Tomoya ^a   Mori, Hiroyuki ^b   Echizen, Yuka ^a   Ishitani, Ryuichiro ^a   Fukai, Shuya ^a   Tanaka, Takeshi ^c   Perederina, Anna ^d   Vassylyev, Dmitry G ^d   Kohno, Toshiyuki ^c   Maturana, Andrés D ^e   Ito, Koreaki ^f   Nureki, Osamu ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b KYOTO UNIVERSITY   (Japan)

^c MITSUBISHI KAGAKU INSTITUTE OF LIFE SCIENCES   (Japan)

^d UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^e NAGAOKA UNIVERSITY OF TECHNOLOGY   (Japan)

^f KYOTO SANGYO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ARGININE; ASPARAGINE; BACTERIAL PROTEIN; PROTEIN SECDF; UNCLASSIFIED DRUG;

BACTERIUM; CRYSTAL STRUCTURE; GENE EXPRESSION; MEMBRANE; MOLECULAR ANALYSIS; PH; PROTEIN;

ARTICLE; CONFORMATIONAL TRANSITION; CYTOPLASM; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; THERMUS THERMOPHILUS;

ADENOSINE TRIPHOSPHATE; ARGININE; ASPARAGINE; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; HYDROGEN-ION CONCENTRATION; MEMBRANE PROTEINS; MEMBRANE TRANSPORT PROTEINS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PERIPLASM; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; PROTEIN UNFOLDING; PROTON-MOTIVE FORCE; STATIC ELECTRICITY; STRUCTURE-ACTIVITY RELATIONSHIP; THERMUS THERMOPHILUS;

BACTERIA (MICROORGANISMS); THERMUS THERMOPHILUS;

EID: 79958281760     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature09980     Document Type: Article

References (27)

1. van den Berg, B. et al. X-ray structure of a protein-conducting channel. Nature 427, 36-44 (2004). (Pubitemid 38094813)
2. Zimmer, J., Nam, Y. Rapoport, T. A. Structure of a complex of the ATPase SecA and the protein-translocation channel. Nature 455, 936-943 (2008).
3. Tsukazaki, T. et al. Conformational transition of Sec machinery inferred from bacterial SecYE structures. Nature 455, 988-991 (2008).
4. du Plessis, D. J., Nouwen, N. Driessen, A. J. The Sec translocase. Biochim. Biophys. Acta 1808, 851-865 (2011).
5. Driessen, A. J. Wickner, W. Proton transfer is rate-limiting for translocation of precursor proteins by the Escherichia coli translocase. Proc. Natl Acad. Sci. USA 88, 2471-2475 (1991). (Pubitemid 21916439)
6. Shiozuka, K., Tani, K., Mizushima, S. Tokuda, H. The proton motive force lowers the level of ATP required for the in vitro translocation of a secretory protein in Escherichia coli. J. Biol. Chem. 265, 18843-18847 (1990).
7. Pogliano, J. A. Beckwith, J. SecD and SecF facilitate protein export in Escherichia coli. EMBO J. 13, 554-561 (1994). (Pubitemid 24050669)
8. Sagara, K., Matsuyama, S. Mizushima, S. SecF stabilizes SecD and SecY, components of the protein translocation machinery of the Escherichia coli cytoplasmic membrane. J. Bacteriol. 176, 4111-4116 (1994). (Pubitemid 24191296)
9. Hand, N. J., Klein, R., Laskewitz, A. Pohlschroder, M. Archaeal and bacterial SecD and SecF homologs exhibit striking structural and functional conservation. J. Bacteriol. 188, 1251-1259 (2006). (Pubitemid 43228657)
10. Matsuyama, S., Fujita, Y. Mizushima, S. SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coli. EMBO J. 12, 265-270 (1993). (Pubitemid 23042403)
11. Economou, A., Pogliano, J. A., Beckwith, J., Oliver, D. B. Wickner, W. SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF. Cell 83, 1171-1181 (1995). (Pubitemid 26007808)
12. Arkowitz, R. A. Wickner, W. SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocation. EMBO J. 13, 954-963 (1994). (Pubitemid 24057528)
13. Duong, F. Wickner, W. The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling. EMBO J. 16, 4871-4879 (1997). (Pubitemid 27348396)
14. Nouwen, N., Piwowarek, M., Berrelkamp, G. Driessen, A. J. The large first periplasmic loop of SecD and SecF plays an important role in SecDF functioning. J. Bacteriol. 187, 5857-5860 (2005). (Pubitemid 41134326)
15. Pogliano, K. J. Beckwith, J. Genetic and molecular characterization of the Escherichia coli secD operon and its products. J. Bacteriol. 176, 804-814 (1994). (Pubitemid 24043970)
16. Tseng, T. T. et al. The RND permease superfamily: an ancient, ubiquitous and diverse family that includes human disease and development proteins. J. Mol. Microbiol. Biotechnol. 1, 107-125 (1999).
17. Tsukazaki, T. et al. Purification, crystallization and preliminary X-ray diffraction of SecDF, a translocon-associated membrane protein, from Thermus thermophilus. Acta Crystallogr. F 62, 376-380 (2006).
18. Uchida, K., Mori, H. Mizushima, S. Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli. J. Biol. Chem. 270, 30862-30868 (1995). (Pubitemid 26012167)
19. Schiebel,E., Driessen,A.J.,Hartl,F.U. Wickner,W. DmH1andATPfunctionatdifferent steps of the catalytic cycle of preprotein translocase. Cell 64, 927-939 (1991).
20. Murakami, S.,Nakashima, R., Yamashita, E.,Matsumoto, T. Yamaguchi, A. Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature 443, 173-179 (2006). (Pubitemid 44387601)
21. Seeger, M. A., von Ballmoos, C., Verrey, F. Pos, K. M. Crucial role of Asp408 in the proton translocation pathway of multidrug transporter AcrB: evidence from sitedirected mutagenesis and carbodiimide labeling. Biochemistry 48, 5801-5812 (2009).
22. Häse, C. C. Barquera, B. Role of sodiumbioenergetics in Vibrio cholerae. Biochim. Biophys. Acta 1505, 169-178 (2001).
23. Sasaki, M., Takagi, M. Okamura, Y. A voltage sensor-domain protein is a voltagegated proton channel. Science 312, 589-592 (2006).
24. Hattori, M. et al. Mg21-dependent gating of bacterial MgtE channel underlies Mg21 homeostasis. EMBO J. 28, 3602-3612 (2009).
25. Vassylyev, D. G. et al. Structural basis for substrate loading in bacterial RNA polymerase. Nature 448, 163-168 (2007). (Pubitemid 47067369)
26. Inaba, K. et al. Crystal structure of the DsbB-DsbA complex reveals amechanismof disulfide bond generation. Cell 127, 789-801 (2006). (Pubitemid 44716258)
27. Matsuo, E., Mori, H., Shimoike, T. Ito, K. Syd, a SecY-interacting protein, excludes SecA from the SecYE complex with an altered SecY24 subunit. J. Biol. Chem. 273, 18835-18840 (1998). (Pubitemid 28366269)