메뉴 건너뛰기




Volumn 57, Issue 2, 2005, Pages 313-317

Ribosome-based protein folding systems are structurally divergent but functionally universal across biological kingdoms

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 70; POLYPEPTIDE; PROTEIN DNAK; RIBOSOME PROTEIN; RIBOSOME PROTEIN L23; TRIGGER FACTOR; UNCLASSIFIED DRUG;

EID: 22144442459     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2005.04696.x     Document Type: Short Survey
Times cited : (12)

References (30)
  • 1
    • 1942421714 scopus 로고    scopus 로고
    • Function of trigger factor and DnaK in multidomain protein folding: Increase in yield at the expense of folding speed
    • Agashe, V.R., Guha, S., Chang, H.C., Genevaux, P., Hayer-Hartl, M., Stemp, M., et al. (2004) Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed. Cell 117: 199-209.
    • (2004) Cell , vol.117 , pp. 199-209
    • Agashe, V.R.1    Guha, S.2    Chang, H.C.3    Genevaux, P.4    Hayer-Hartl, M.5    Stemp, M.6
  • 2
    • 14544275165 scopus 로고    scopus 로고
    • From peptide-bond formation to cotranslational folding: Dynamic, regulatory and evolutionary aspects
    • Baram, D., and Yonath, A. (2005) From peptide-bond formation to cotranslational folding: dynamic, regulatory and evolutionary aspects. FEBS Lett 579: 948-954.
    • (2005) FEBS Lett , vol.579 , pp. 948-954
    • Baram, D.1    Yonath, A.2
  • 3
    • 2542614508 scopus 로고    scopus 로고
    • Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor
    • Buskiewicz, I., Deuerling, E., Gu, S.Q., Jockel, J., Rodnina, M.V., Bukau, B., and Wintermeyer, W. (2004) Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor. Proc Natl Acad Sci USA 101: 7902-7906.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7902-7906
    • Buskiewicz, I.1    Deuerling, E.2    Gu, S.Q.3    Jockel, J.4    Rodnina, M.V.5    Bukau, B.6    Wintermeyer, W.7
  • 4
    • 0023387587 scopus 로고
    • Trigger factor: A soluble protein that folds pro-OmpA into a membrane-assembly-competent form
    • Crooke, E., and Wickner, W. (1987) Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form. Proc Natl Acad Sci USA 84: 5216-5220.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5216-5220
    • Crooke, E.1    Wickner, W.2
  • 5
    • 11444271010 scopus 로고    scopus 로고
    • Chaperone-assisted folding of newly synthesized proteins in the cytosol
    • Deuerling, E., and Bukau, B. (2004) Chaperone-assisted folding of newly synthesized proteins in the cytosol. Crit Rev Biochem Mol Biol 39: 261-277.
    • (2004) Crit Rev Biochem Mol Biol , vol.39 , pp. 261-277
    • Deuerling, E.1    Bukau, B.2
  • 6
    • 0033549770 scopus 로고    scopus 로고
    • Trigger factor and DnaK cooperate in folding of newly synthesized proteins
    • Deuerling, E., Schulze-Specking, A., Tomoyasu, T., Mogk, A., and Bukau, B. (1999) Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Nature 400: 693-696.
    • (1999) Nature , vol.400 , pp. 693-696
    • Deuerling, E.1    Schulze-Specking, A.2    Tomoyasu, T.3    Mogk, A.4    Bukau, B.5
  • 8
    • 4944246094 scopus 로고    scopus 로고
    • Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
    • Ferbitz, L., Maier, T., Patzelt, H., Bukau, B., Deuerling, E., and Ban, N. (2004) Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. Nature 431: 590-596.
    • (2004) Nature , vol.431 , pp. 590-596
    • Ferbitz, L.1    Maier, T.2    Patzelt, H.3    Bukau, B.4    Deuerling, E.5    Ban, N.6
  • 9
    • 0037007060 scopus 로고    scopus 로고
    • A functional chaperone triad on the yeast ribosome
    • Gautschi, M., Mun, A., Ross, S., and Rospert, S. (2002) A functional chaperone triad on the yeast ribosome. Proc Natl Acad Sci USA 99: 4209-4214.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4209-4214
    • Gautschi, M.1    Mun, A.2    Ross, S.3    Rospert, S.4
  • 11
    • 0029913836 scopus 로고    scopus 로고
    • Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains
    • Hesterkamp, T., Hauser, S., Lutcke, H., and Bukau, B. (1996) Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. Proc Natl Acad Sci USA 93: 4437-4441.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4437-4441
    • Hesterkamp, T.1    Hauser, S.2    Lutcke, H.3    Bukau, B.4
  • 12
    • 0037007008 scopus 로고    scopus 로고
    • The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain
    • Hundley, H., Eisenman, H., Walter, W., Evans, T., Hotokezaka, Y., Wiedmann, M., and Craig, E. (2002) The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain. Proc Natl Acad Sci USA 99: 4203-4208.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4203-4208
    • Hundley, H.1    Eisenman, H.2    Walter, W.3    Evans, T.4    Hotokezaka, Y.5    Wiedmann, M.6    Craig, E.7
  • 13
    • 18644382616 scopus 로고    scopus 로고
    • Human Mpp11 J protein: Ribosome-tethered molecular chaperones are ubiquitous
    • Hundley, H.A., Walter, W., Bairstow, S., and Craig, E.A. (2005) Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous. Science 38: 1032-1034.
    • (2005) Science , vol.38 , pp. 1032-1034
    • Hundley, H.A.1    Walter, W.2    Bairstow, S.3    Craig, E.A.4
  • 14
    • 0037399205 scopus 로고    scopus 로고
    • The chemistry of protein synthesis and voyage through the ribosomal tunnel
    • Jenni, S., and Ban, N. (2003) The chemistry of protein synthesis and voyage through the ribosomal tunnel. Curr Opin Struct Biol 13: 212-219.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 212-219
    • Jenni, S.1    Ban, N.2
  • 15
    • 13744258264 scopus 로고    scopus 로고
    • Broad sensitivity of Saccharomyces cerevisiae lacking ribosome-associated chaperone ssb or zuo1 to cations, including aminoglycosides
    • Kim, S.Y., and Craig, E.A. (2005) Broad sensitivity of Saccharomyces cerevisiae lacking ribosome-associated chaperone ssb or zuo1 to cations, including aminoglycosides. Eukaryot Cell 4: 82-89.
    • (2005) Eukaryot Cell , vol.4 , pp. 82-89
    • Kim, S.Y.1    Craig, E.A.2
  • 17
    • 1842639447 scopus 로고    scopus 로고
    • Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli
    • Kramer, G., Patzelt, H., Rauch, T., Kurz, T.A., Vorderwulbecke, S., Bukau, B., and Deuerling, E. (2004) Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli. J Biol Chem 279: 14165-14170.
    • (2004) J Biol Chem , vol.279 , pp. 14165-14170
    • Kramer, G.1    Patzelt, H.2    Rauch, T.3    Kurz, T.A.4    Vorderwulbecke, S.5    Bukau, B.6    Deuerling, E.7
  • 18
    • 0037044752 scopus 로고    scopus 로고
    • Trigger factor retards protein export in Escherichia coli
    • Lee, H.C., and Bernstein, H.D. (2002) Trigger factor retards protein export in Escherichia coli. J Biol Chem 277: 43527-43535.
    • (2002) J Biol Chem , vol.277 , pp. 43527-43535
    • Lee, H.C.1    Bernstein, H.D.2
  • 19
    • 8844239874 scopus 로고    scopus 로고
    • SRP-mediated protein targeting: Structure and function revisited
    • Luirink, J., and Sinning, I. (2004) SRP-mediated protein targeting: structure and function revisited. FEBS Lett 1694: 17-35.
    • (2004) FEBS Lett , vol.1694 , pp. 17-35
    • Luirink, J.1    Sinning, I.2
  • 20
    • 4344668509 scopus 로고    scopus 로고
    • Translation arrest of SecM is essential for the basal and regulated expression of SecA
    • Murakami, A., Nakatogawa, H., and Ito, K. (2004) Translation arrest of SecM is essential for the basal and regulated expression of SecA. Proc Natl Acad Sci USA 101: 12330-12335.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12330-12335
    • Murakami, A.1    Nakatogawa, H.2    Ito, K.3
  • 22
    • 0035658334 scopus 로고    scopus 로고
    • Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared with other Hsp70s
    • Pfund, C., Huang, P., Lopez-Hoyo, N., and Craig, E.A. (2001) Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared with other Hsp70s. Mol Biol Cell 12: 3773-3782.
    • (2001) Mol Biol Cell , vol.12 , pp. 3773-3782
    • Pfund, C.1    Huang, P.2    Lopez-Hoyo, N.3    Craig, E.A.4
  • 23
    • 4744374703 scopus 로고    scopus 로고
    • The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae
    • Rakwalska, M., and Rospert, S. (2004) The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae. Mol Cell Biol 24: 9186-9197.
    • (2004) Mol Cell Biol , vol.24 , pp. 9186-9197
    • Rakwalska, M.1    Rospert, S.2
  • 24
    • 22144451849 scopus 로고    scopus 로고
    • Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli
    • doi:10.1111/j/1365-2958.2005.04690.x
    • Rauch, T., Hundley, H.A., Pfund, C., Wegrzyn, R.D., Walter, W., Kramer, G., et al. (2005) Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli. Mol Microbiol, doi:10.1111/j/1365-2958.2005.04690.x
    • (2005) Mol Microbiol
    • Rauch, T.1    Hundley, H.A.2    Pfund, C.3    Wegrzyn, R.D.4    Walter, W.5    Kramer, G.6
  • 25
    • 0028864461 scopus 로고
    • A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor
    • Stoller, G., Rucknagel, K.P., Nierhaus, K.H., Schmid, F.X., Fischer, G., and Rahfeld, J.U. (1995) A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor. EMBO J 14: 4939-4948.
    • (1995) EMBO J , vol.14 , pp. 4939-4948
    • Stoller, G.1    Rucknagel, K.P.2    Nierhaus, K.H.3    Schmid, F.X.4    Fischer, G.5    Rahfeld, J.U.6
  • 26
    • 0033032592 scopus 로고    scopus 로고
    • Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains
    • Teter, S.A., Houry, W.A., Ang, D., Tradler, T., Rockabrand, D., Fischer, G., et al. (1999) Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains. Cell 97: 755-765.
    • (1999) Cell , vol.97 , pp. 755-765
    • Teter, S.A.1    Houry, W.A.2    Ang, D.3    Tradler, T.4    Rockabrand, D.5    Fischer, G.6
  • 28
    • 0028799459 scopus 로고
    • Early events in preprotein recognition in E. coli: Interaction of SRP and trigger factor with nascent polypeptides
    • Valent, Q.A., Kendall, D.A., High, S., Kusters, R., Oudega, B., and Luirink, J. (1995) Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides. EMBO J 14: 5494-5505.
    • (1995) EMBO J , vol.14 , pp. 5494-5505
    • Valent, Q.A.1    Kendall, D.A.2    High, S.3    Kusters, R.4    Oudega, B.5    Luirink, J.6
  • 29
    • 0442307793 scopus 로고    scopus 로고
    • Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK
    • Vorderwulbecke, S., Kramer, G., Merz, F., Kurz, T.A., Rauch, T., Zachmann-Brand, B., et al. (2004) Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK. FEBS Lett 559: 181-187.
    • (2004) FEBS Lett , vol.559 , pp. 181-187
    • Vorderwulbecke, S.1    Kramer, G.2    Merz, F.3    Kurz, T.A.4    Rauch, T.5    Zachmann-Brand, B.6
  • 30
    • 1542358892 scopus 로고    scopus 로고
    • Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins
    • Woolhead, C.A., McCormick, P.J., and Johnson, A.E. (2004) Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins. Cell 116: 725-736.
    • (2004) Cell , vol.116 , pp. 725-736
    • Woolhead, C.A.1    McCormick, P.J.2    Johnson, A.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.