메뉴 건너뛰기




Volumn 80, Issue 2, 2015, Pages 172-179

Effect of chaperonin encoded by gene 146 on thermal aggregation of lytic proteins of bacteriophage EL Pseudomonas aeruginosa

Author keywords

bacteriophage EL; endolysin; phage chaperonin; protein aggregation

Indexed keywords

PSEUDOMONAS AERUGINOSA;

EID: 84923325003     PISSN: 00062979     EISSN: 16083040     Source Type: Journal    
DOI: 10.1134/S0006297915020042     Document Type: Article
Times cited : (10)

References (22)
  • 1
    • 84882425518 scopus 로고    scopus 로고
    • Chaperonin-mediated protein folding
    • 1:CAS:528:DC%2BC3sXht1yhsr7J 23803606
    • Horwich, A. L. (2013) Chaperonin-mediated protein folding, J. Biol. Chem., 288, 23622-23632.
    • (2013) J. Biol. Chem. , vol.288 , pp. 23622-23632
    • Horwich, A.L.1
  • 2
    • 28844440537 scopus 로고    scopus 로고
    • Characterization of archaeal group II chaperonin-ADP-metal fluoride complexes: Implications that group II chaperonins operate as a "two-stroke engine"
    • 1:CAS:528:DC%2BD2MXht1Gjs7jM 16183634
    • Iizuka, R., Yoshida, T., Ishii, N., Zako, T., Takahashi, K., Maki, K., Inobe, T., Kuwajima, K., and Yohda, M. (2005) Characterization of archaeal group II chaperonin-ADP-metal fluoride complexes: implications that group II chaperonins operate as a "two-stroke engine", J. Biol. Chem., 280, 40375-40383.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40375-40383
    • Iizuka, R.1    Yoshida, T.2    Ishii, N.3    Zako, T.4    Takahashi, K.5    Maki, K.6    Inobe, T.7    Kuwajima, K.8    Yohda, M.9
  • 3
    • 0015915068 scopus 로고
    • Host participation in bacteriophage lambda head assembly
    • 1:STN:280:DyaE3s3hvVGnsA%3D%3D 4578100
    • Georgopoulos, C. P., Hendrix, R. W., Casjens, S. R., and Kaiser, A. D. (1973) Host participation in bacteriophage lambda head assembly, J. Mol. Biol., 76, 45-60.
    • (1973) J. Mol. Biol. , vol.76 , pp. 45-60
    • Georgopoulos, C.P.1    Hendrix, R.W.2    Casjens, S.R.3    Kaiser, A.D.4
  • 4
    • 0028240858 scopus 로고
    • Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding
    • Van der Vies, S. M., Gatenby, A. A., and Georgopoulos, C. (1994) Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding, Nature, 368, 654-656.
    • (1994) Nature , vol.368 , pp. 654-656
    • Van Der Vies, S.M.1    Gatenby, A.A.2    Georgopoulos, C.3
  • 5
    • 0035937860 scopus 로고    scopus 로고
    • Pseudo-T-even bacteriophage RB49 encodes CocO, a cochaperonin for GroEL, which can substitute for Escherichia coli's GroES and bacteriophage T4's gp31
    • 1:CAS:528:DC%2BD3MXisVCnsbY%3D 11104767
    • Ang, D., Richardson, A., Mayer, M. P., Keppel, F., Krisch, H., and Georgopoulos, C. (2001) Pseudo-T-even bacteriophage RB49 encodes CocO, a cochaperonin for GroEL, which can substitute for Escherichia coli's GroES and bacteriophage T4's gp31, J. Biol. Chem., 276, 8720-8726.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8720-8726
    • Ang, D.1    Richardson, A.2    Mayer, M.P.3    Keppel, F.4    Krisch, H.5    Georgopoulos, C.6
  • 7
    • 29244485920 scopus 로고    scopus 로고
    • Yersiniophage phiR1-37 is a tailed bacteriophage having a 270 kb DNA genome with thymidine replaced by deoxyuridine
    • 1:CAS:528:DC%2BD28Xhslyntw%3D%3D 16339954
    • Kiljunen, S., Hakala, K., Pinta, E., Huttunen, S., Pluta, P., Gador, A., Lönnberg, H., and Skurnik, M. (2005) Yersiniophage phiR1-37 is a tailed bacteriophage having a 270 kb DNA genome with thymidine replaced by deoxyuridine, Microbiology, 151, 4093-4102.
    • (2005) Microbiology , vol.151 , pp. 4093-4102
    • Kiljunen, S.1    Hakala, K.2    Pinta, E.3    Huttunen, S.4    Pluta, P.5    Gador, A.6    Lönnberg, H.7    Skurnik, M.8
  • 8
    • 84857071796 scopus 로고    scopus 로고
    • Complete genome sequence of the giant virus OBP and comparative genome analysis of the diverse φkZ-related phages
    • 1:CAS:528:DC%2BC38XhsV2nu7Y%3D 22130535
    • Cornelissen, A., Hardies, S. C., Shaburova, O. V., Krylov, V. N., Mattheus, W., Kropinski, A. M., and Lavigne, R. (2012) Complete genome sequence of the giant virus OBP and comparative genome analysis of the diverse φKZ-related phages, J. Virol., 86, 1844-1852.
    • (2012) J. Virol. , vol.86 , pp. 1844-1852
    • Cornelissen, A.1    Hardies, S.C.2    Shaburova, O.V.3    Krylov, V.N.4    Mattheus, W.5    Kropinski, A.M.6    Lavigne, R.7
  • 9
    • 84887145578 scopus 로고    scopus 로고
    • Phylogenomic network and comparative genomics reveal a diverged member of the φkZ-related group, marine vibrio phage φjM-2012
    • 1:CAS:528:DC%2BC3sXhvVygsrvL 24067958
    • Jang, H. B., Fagutao, F. F., Nho, S. W., Park, S. B., Cha, I. S., Yu, J. E., Lee, J. S., Im, S. P., Aoki, T., and Jung, T. S. (2013) Phylogenomic network and comparative genomics reveal a diverged member of the φKZ-related group, marine vibrio phage φJM-2012, J. Virol., 87, 12866-12878.
    • (2013) J. Virol. , vol.87 , pp. 12866-12878
    • Jang, H.B.1    Fagutao, F.F.2    Nho, S.W.3    Park, S.B.4    Cha, I.S.5    Yu, J.E.6    Lee, J.S.7    Im, S.P.8    Aoki, T.9    Jung, T.S.10
  • 10
    • 84866155404 scopus 로고    scopus 로고
    • Expression and functional characterization of the first bacteriophage-encoded chaperonin
    • 1:CAS:528:DC%2BC38XhtlChsL3E 22787217
    • Kurochkina, L. P., Semenyuk, P. I., Orlov, V. N., Robben, J., Sykilinda, N. N., and Mesyanzhinov, V. V. (2012) Expression and functional characterization of the first bacteriophage-encoded chaperonin, J. Virol., 86, 10103-10111.
    • (2012) J. Virol. , vol.86 , pp. 10103-10111
    • Kurochkina, L.P.1    Semenyuk, P.I.2    Orlov, V.N.3    Robben, J.4    Sykilinda, N.N.5    Mesyanzhinov, V.V.6
  • 11
    • 33847633917 scopus 로고    scopus 로고
    • A standardized approach for accurate quantification of murein hydrolase activity in high-throughput assays
    • 1:CAS:528:DC%2BD2sXislKjtLo%3D 17169435
    • Briers, Y., Lavigne, R., Volckaert, G., and Hertveldt, K. (2007) A standardized approach for accurate quantification of murein hydrolase activity in high-throughput assays, J. Biochem. Biophys. Methods, 70, 531-533.
    • (2007) J. Biochem. Biophys. Methods , vol.70 , pp. 531-533
    • Briers, Y.1    Lavigne, R.2    Volckaert, G.3    Hertveldt, K.4
  • 12
    • 0034265484 scopus 로고    scopus 로고
    • Structure and folding of bacteriophage T4 gene product 9 triggering infection. II. Study of conformational changes of gene product 9 mutants using monoclonal antibodies
    • 1:CAS:528:DC%2BD3cXntlOltLs%3D
    • Zhemaeva, L. V., Sykilinda, N. N., Navruzbekov, G. A., Kurochkina, L. P., and Mesyanzhinov, V. V. (2000) Structure and folding of bacteriophage T4 gene product 9 triggering infection. II. Study of conformational changes of gene product 9 mutants using monoclonal antibodies, Biochemistry (Moscow), 65, 1068-1074.
    • (2000) Biochemistry (Moscow) , vol.65 , pp. 1068-1074
    • Zhemaeva, L.V.1    Sykilinda, N.N.2    Navruzbekov, G.A.3    Kurochkina, L.P.4    Mesyanzhinov, V.V.5
  • 15
    • 0001665043 scopus 로고
    • Limits of the fractal dimension for irreversible kinetic aggregation of gold colloids
    • 1:CAS:528:DyaL2MXhvFWrurY%3D 10031026
    • Weitz, D. A., Huang, J. S., Lin, M. Y., and Sung, J. (1985) Limits of the fractal dimension for irreversible kinetic aggregation of gold colloids, Phys. Rev. Lett., 54, 1416-1419.
    • (1985) Phys. Rev. Lett. , vol.54 , pp. 1416-1419
    • Weitz, D.A.1    Huang, J.S.2    Lin, M.Y.3    Sung, J.4
  • 17
    • 0023917654 scopus 로고
    • A malachite green procedure for orthophosphate determination and its use in alkaline phosphatase-based enzyme immunoassay
    • 1:STN:280:DyaL1czgsl2juw%3D%3D 3044186
    • Baykov, A. A., Evtushenko, O. A., and Avaeva, S. M. (1988) A malachite green procedure for orthophosphate determination and its use in alkaline phosphatase-based enzyme immunoassay, Anal. Biochem., 171, 266-270.
    • (1988) Anal. Biochem. , vol.171 , pp. 266-270
    • Baykov, A.A.1    Evtushenko, O.A.2    Avaeva, S.M.3
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 1:CAS:528:DC%2BD3MXlsFags7s%3D 5432063
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 75049084608 scopus 로고    scopus 로고
    • Comparative analysis of the effects of α-crystallin and GroEL on the kinetics of thermal aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase
    • 1:CAS:528:DC%2BD1MXhsVCqurfK 19936900
    • Markossian, K. A., Golub, N. V., Chebotareva, N. A., Asryants, R. A., Naletova, I. N., Muronetz, V. I., Muranov, K. O., and Kurganov, B. I. (2010) Comparative analysis of the effects of α-crystallin and GroEL on the kinetics of thermal aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase, Protein J., 29, 11-25.
    • (2010) Protein J. , vol.29 , pp. 11-25
    • Markossian, K.A.1    Golub, N.V.2    Chebotareva, N.A.3    Asryants, R.A.4    Naletova, I.N.5    Muronetz, V.I.6    Muranov, K.O.7    Kurganov, B.I.8
  • 20
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • 1:CAS:528:DC%2BD38XhvFClsL4%3D 11884745
    • Hartl, F. U., and Hayer-Hartl, M. (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein, Science, 295, 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 21
    • 78649602176 scopus 로고    scopus 로고
    • Analysis of peptides and proteins in their binding to GroEL
    • 1:CAS:528:DC%2BC3cXhsVGitbfO 20814869
    • Li, Y., Zheng, Z., Ramsey, A., and Chen, L. (2010) Analysis of peptides and proteins in their binding to GroEL, J. Pept. Sci., 16, 693-700.
    • (2010) J. Pept. Sci. , vol.16 , pp. 693-700
    • Li, Y.1    Zheng, Z.2    Ramsey, A.3    Chen, L.4
  • 22
    • 0032701797 scopus 로고    scopus 로고
    • Group II chaperonins: New TRiC(k)s and turns of a protein folding machine
    • 1:CAS:528:DyaK1MXms12rtLg%3D 10550210
    • Gutsche, I., Essen, L. O., and Baumeister, W. (1999) Group II chaperonins: new TRiC(k)s and turns of a protein folding machine, J. Mol. Biol., 293, 295-312.
    • (1999) J. Mol. Biol. , vol.293 , pp. 295-312
    • Gutsche, I.1    Essen, L.O.2    Baumeister, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.