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Volumn 84, Issue 6, 2018, Pages

A cytoplasmic antiholin is embedded in frame with the holin in a Lactobacillus fermentum bacteriophage

Author keywords

Antiholin; Bacteriophage; Holin; Lactic acid bacteria; Lactobacillus fermentum

Indexed keywords

ACTIVATION ANALYSIS; AMINO ACIDS; ENCODING (SYMBOLS); ESCHERICHIA COLI; GENE ENCODING; GENES; LACTIC ACID; PLANTS (BOTANY); SIGNAL ENCODING;

EID: 85042678319     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02518-17     Document Type: Article
Times cited : (10)

References (36)
  • 1
    • 84957729059 scopus 로고    scopus 로고
    • Mycobacteriophage D29 holin C-terminal region functionally assists in holin aggregation and bacterial cell death
    • Kamilla S, Jain V. 2016. Mycobacteriophage D29 holin C-terminal region functionally assists in holin aggregation and bacterial cell death. FEBS J 283:173-190. https://doi.org/10.1111/febs.13565
    • (2016) FEBS J , vol.283 , pp. 173-190
    • Kamilla, S.1    Jain, V.2
  • 2
    • 1642390837 scopus 로고    scopus 로고
    • Distribution and composition of the lysis cassette of Lactococcus lactis phages and functional analysis of bacteriophage ul36 holin
    • Labrie S, Vukov N, Loessner MJ, Moineau S. 2004. Distribution and composition of the lysis cassette of Lactococcus lactis phages and functional analysis of bacteriophage ul36 holin. FEMS Microbiol Lett 233: 37-43. https://doi.org/10.1016/j.femsle.2004.01.038
    • (2004) FEMS Microbiol Lett , vol.233 , pp. 37-43
    • Labrie, S.1    Vukov, N.2    Loessner, M.J.3    Moineau, S.4
  • 3
    • 56649097462 scopus 로고    scopus 로고
    • Identification and characterization of the two-component cell lysis cassette encoded by temperate bacteriophage phiPYB5 of Lactobacillus fermentum
    • Wang S, Kong J, Zhang X. 2008. Identification and characterization of the two-component cell lysis cassette encoded by temperate bacteriophage phiPYB5 of Lactobacillus fermentum. J Appl Microbiol 105:1939-1944. https://doi.org/10.1111/j.1365-2672.2008.03953.x
    • (2008) J Appl Microbiol , vol.105 , pp. 1939-1944
    • Wang, S.1    Kong, J.2    Zhang, X.3
  • 4
    • 34548730347 scopus 로고    scopus 로고
    • Subclassification and targeted characterization of prophage-encoded two-component cell lysis cassette
    • Srividhya KV, Krishnaswamy S. 2007. Subclassification and targeted characterization of prophage-encoded two-component cell lysis cassette. J Biosci 32:979-990. https://doi.org/10.1007/s12038-007-0097-x
    • (2007) J Biosci , vol.32 , pp. 979-990
    • Srividhya, K.V.1    Krishnaswamy, S.2
  • 5
    • 84895198685 scopus 로고    scopus 로고
    • Phage lysis: three steps, three choices, one outcome
    • Young R. 2014. Phage lysis: three steps, three choices, one outcome. J Microbiol 52:243-258. https://doi.org/10.1007/s12275-014-4087-z
    • (2014) J Microbiol , vol.52 , pp. 243-258
    • Young, R.1
  • 6
    • 79958281245 scopus 로고    scopus 로고
    • A second endolysin gene is fully embedded in-frame with the lysA gene of mycobacteriophage Ms6
    • Catalao MJ, Milho C, Gil F, Moniz-Pereira J, Pimentel M. 2011. A second endolysin gene is fully embedded in-frame with the lysA gene of mycobacteriophage Ms6. PLoS One 6:e20515. https://doi.org/10.1371/journal.pone.0020515
    • (2011) PLoS One , vol.6
    • Catalao, M.J.1    Milho, C.2    Gil, F.3    Moniz-Pereira, J.4    Pimentel, M.5
  • 7
    • 2342634418 scopus 로고    scopus 로고
    • A signal-arrestrelease sequence mediates export and control of the phage P1 endolysin
    • Xu M, Struck DK, Swanson S, Sacchettini JC. 2004. A signal-arrestrelease sequence mediates export and control of the phage P1 endolysin. Proc Natl Acad Sci U S A 101:6415-6420. https://doi.org/10.1073/pnas.0400957101
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 6415-6420
    • Xu, M.1    Struck, D.K.2    Swanson, S.3    Sacchettini, J.C.4
  • 8
    • 0037121070 scopus 로고    scopus 로고
    • Molecular analysis of the lysis protein Lys encoded by Lactobacillus plantarum phage phig1e
    • Kakikawa M, Yokoi KJ, Kimoto H, Nakano M, Kawasaki K, Taketo A, Kodaira K. 2002. Molecular analysis of the lysis protein Lys encoded by Lactobacillus plantarum phage phig1e. Gene 299:227-234. https://doi .org/10.1016/S0378-1119(02)01076-4
    • (2002) Gene , vol.299 , pp. 227-234
    • Kakikawa, M.1    Yokoi, K.J.2    Kimoto, H.3    Nakano, M.4    Kawasaki, K.5    Taketo, A.6    Kodaira, K.7
  • 9
    • 84924538811 scopus 로고    scopus 로고
    • Functional analysis of the N-terminal region of endolysin Lyb5 encoded by Lactobacillus fermentum bacteriophage phiPYB5
    • Guo T, Zhang C, Liu W, Wang S, Kong J. 2015. Functional analysis of the N-terminal region of endolysin Lyb5 encoded by Lactobacillus fermentum bacteriophage phiPYB5. Int J Food Microbiol 203:1-7. https://doi .org/10.1016/j.ijfoodmicro.2015.02.033
    • (2015) Int J Food Microbiol , vol.203 , pp. 1-7
    • Guo, T.1    Zhang, C.2    Liu, W.3    Wang, S.4    Kong, J.5
  • 10
    • 0037310365 scopus 로고    scopus 로고
    • Sizing the holin lesion with an endolysin-beta-galactosidase fusion
    • Wang IN, Deaton J, Young R. 2003. Sizing the holin lesion with an endolysin-beta-galactosidase fusion. J Bacteriol 185:779-787. https://doi .org/10.1128/JB.185.3.779-787.2003
    • (2003) J Bacteriol , vol.185 , pp. 779-787
    • Wang, I.N.1    Deaton, J.2    Young, R.3
  • 11
    • 79958121285 scopus 로고    scopus 로고
    • Functional analysis of the holin-like proteins of mycobacteriophage Ms6
    • Catalão MJ, Gil F, Moniz-Pereira J, Pimentel M. 2011. Functional analysis of the holin-like proteins of mycobacteriophage Ms6. J Bacteriol 193: 2793-2803. https://doi.org/10.1128/JB.01519-10
    • (2011) J Bacteriol , vol.193 , pp. 2793-2803
    • Catalão, M.J.1    Gil, F.2    Moniz-Pereira, J.3    Pimentel, M.4
  • 12
    • 37449031844 scopus 로고    scopus 로고
    • The pinholin of lambdoid phage 21: control of lysis by membrane depolarization
    • Park T, Struck DK, Dankenbring CA, Young R. 2007. The pinholin of lambdoid phage 21: control of lysis by membrane depolarization. J Bacteriol 189:9135-9139. https://doi.org/10.1128/JB.00847-07
    • (2007) J Bacteriol , vol.189 , pp. 9135-9139
    • Park, T.1    Struck, D.K.2    Dankenbring, C.A.3    Young, R.4
  • 14
    • 0036132523 scopus 로고    scopus 로고
    • Bacteriophage holins: deadly diversity
    • Young R. 2002. Bacteriophage holins: deadly diversity. J Mol Microbiol Biotechnol 4:21-36
    • (2002) J Mol Microbiol Biotechnol , vol.4 , pp. 21-36
    • Young, R.1
  • 15
    • 33845940948 scopus 로고    scopus 로고
    • Topological dynamics of holins in programmed bacterial lysis
    • Park T, Struck DK, Deaton JF, Young R. 2006. Topological dynamics of holins in programmed bacterial lysis. Proc Natl Acad Sci U S A 103: 19713-19718. https://doi.org/10.1073/pnas.0600943103
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 19713-19718
    • Park, T.1    Struck, D.K.2    Deaton, J.F.3    Young, R.4
  • 16
    • 84907821967 scopus 로고    scopus 로고
    • Probing the structure of the S105 hole
    • To KH, Young R. 2014. Probing the structure of the S105 hole. J Bacteriol 196:3683-3689. https://doi.org/10.1128/JB.01673-14
    • (2014) J Bacteriol , vol.196 , pp. 3683-3689
    • To, K.H.1    Young, R.2
  • 17
    • 84862832409 scopus 로고    scopus 로고
    • Characterization and determination of holin protein of Streptococcus suis bacteriophage SMP in heterologous host
    • Shi Y, Yan Y, Ji W, Du BV, Meng X, Wang H, Sun J. 2012. Characterization and determination of holin protein of Streptococcus suis bacteriophage SMP in heterologous host. Virol J 9:70. https://doi.org/10.1186/1743-422X-9-70
    • (2012) Virol J , vol.9 , pp. 70
    • Shi, Y.1    Yan, Y.2    Ji, W.3    Du, B.V.4    Meng, X.5    Wang, H.6    Sun, J.7
  • 18
    • 0035819875 scopus 로고    scopus 로고
    • Genetic analysis of the T4 holin: timing and topology
    • Ramanculov E, Young R. 2001. Genetic analysis of the T4 holin: timing and topology. Gene 265:25-36. https://doi.org/10.1016/S0378-1119(01) 00365-1
    • (2001) Gene , vol.265 , pp. 25-36
    • Ramanculov, E.1    Young, R.2
  • 19
    • 33644778734 scopus 로고    scopus 로고
    • Lysis timing and bacteriophage fitness
    • Wang IN. 2006. Lysis timing and bacteriophage fitness. Genetics 172: 17-26
    • (2006) Genetics , vol.172 , pp. 17-26
    • Wang, I.N.1
  • 20
    • 0033768655 scopus 로고    scopus 로고
    • Holins: the protein clocks of bacteriophage infections
    • Wang IN, Smith DL, Young R. 2000. Holins: the protein clocks of bacteriophage infections. Annu Rev Microbiol 54:799-825. https://doi.org/10 .1146/annurev.micro.54.1.799
    • (2000) Annu Rev Microbiol , vol.54 , pp. 799-825
    • Wang, I.N.1    Smith, D.L.2    Young, R.3
  • 21
    • 75149113312 scopus 로고    scopus 로고
    • The N-terminal transmembrane domain of lambda S is required for holin but not antiholin function
    • White R, Tran TA, Dankenbring CA, Deaton J, Young R. 2010. The N-terminal transmembrane domain of lambda S is required for holin but not antiholin function. J Bacteriol 192:725-733. https://doi.org/10.1128/JB.01263-09
    • (2010) J Bacteriol , vol.192 , pp. 725-733
    • White, R.1    Tran, T.A.2    Dankenbring, C.A.3    Deaton, J.4    Young, R.5
  • 22
    • 0345269852 scopus 로고    scopus 로고
    • Functional regulation of the Listeria monocytogenes bacteriophage A118 holin by an intragenic inhibitor lacking the first transmembrane domain
    • Vukov N, Moll I, Bläsi U, Scherer S, Loessner MJ. 2003. Functional regulation of the Listeria monocytogenes bacteriophage A118 holin by an intragenic inhibitor lacking the first transmembrane domain. Mol Microbiol 48:173-186. https://doi.org/10.1046/j.1365-2958.2003.03421.x
    • (2003) Mol Microbiol , vol.48 , pp. 173-186
    • Vukov, N.1    Moll, I.2    Bläsi, U.3    Scherer, S.4    Loessner, M.J.5
  • 23
    • 35648978139 scopus 로고    scopus 로고
    • The T4 RI antiholin has an N-terminal signal anchor release domain that targets it for degradation by DegP
    • Tran TA, Struck DK, Young R. 2007. The T4 RI antiholin has an N-terminal signal anchor release domain that targets it for degradation by DegP. J Bacteriol 189:7618-7625. https://doi.org/10.1128/JB.00854-07
    • (2007) J Bacteriol , vol.189 , pp. 7618-7625
    • Tran, T.A.1    Struck, D.K.2    Young, R.3
  • 24
    • 25144505528 scopus 로고    scopus 로고
    • Periplasmic domains define holinantiholin interactions in t4 lysis inhibition
    • Tran TA, Struck DK, Young R. 2005. Periplasmic domains define holinantiholin interactions in t4 lysis inhibition. J Bacteriol 187:6631-6640. https://doi.org/10.1128/JB.187.19.6631-6640.2005
    • (2005) J Bacteriol , vol.187 , pp. 6631-6640
    • Tran, T.A.1    Struck, D.K.2    Young, R.3
  • 25
    • 80052248928 scopus 로고    scopus 로고
    • Bacteriophages of lactic acid bacteria and their impact on milk fermentations
    • Garneau JE, Moineau S. 2011. Bacteriophages of lactic acid bacteria and their impact on milk fermentations. Microb Cell Fact 10(Suppl 1):S20. https://doi.org/10.1186/1475-2859-10-S1-S20
    • (2011) Microb Cell Fact , vol.10
    • Garneau, J.E.1    Moineau, S.2
  • 28
    • 33748680714 scopus 로고    scopus 로고
    • Isolation and characterization of a Lactobacillus fermentum temperate bacteriophage from Chinese yogurt
    • Zhang X, Kong J, Qu Y. 2006. Isolation and characterization of a Lactobacillus fermentum temperate bacteriophage from Chinese yogurt. J Appl Microbiol 101:857-863. https://doi.org/10.1111/j.1365-2672.2006 .03007.x
    • (2006) J Appl Microbiol , vol.101 , pp. 857-863
    • Zhang, X.1    Kong, J.2    Qu, Y.3
  • 29
    • 78650036157 scopus 로고    scopus 로고
    • Genome analysis of Lactobacillus fermentum temperate bacteriophage βPYB5
    • Zhang X, Wang S, Guo T, Kong J. 2011. Genome analysis of Lactobacillus fermentum temperate bacteriophage βPYB5. Int J Food Microbiol 144: 400-405. https://doi.org/10.1016/j.ijfoodmicro.2010.10.026
    • (2011) Int J Food Microbiol , vol.144 , pp. 400-405
    • Zhang, X.1    Wang, S.2    Guo, T.3    Kong, J.4
  • 30
    • 0030827371 scopus 로고    scopus 로고
    • Functional and structural features of the holin HOL protein of the Lactobacillus plantarum phage phi gle: analysis in Escherichia coli system
    • Oki M, Kakikawa M, Nakamura S, Yamaura ET, Watanabe K, Sasamoto M, Taketo A, Kodaira K. 1997. Functional and structural features of the holin HOL protein of the Lactobacillus plantarum phage phi gle: analysis in Escherichia coli system. Gene 197:137-145. https://doi.org/10.1016/S0378-1119(97)00252-7
    • (1997) Gene , vol.197 , pp. 137-145
    • Oki, M.1    Kakikawa, M.2    Nakamura, S.3    Yamaura, E.T.4    Watanabe, K.5    Sasamoto, M.6    Taketo, A.7    Kodaira, K.8
  • 31
    • 0028954627 scopus 로고
    • Primary structure and functional analysis of the lysis genes of Lactobacillus gasseri bacteriophage phi adh
    • Henrich B, Binishofer B, Bläsi U. 1995. Primary structure and functional analysis of the lysis genes of Lactobacillus gasseri bacteriophage phi adh. J Bacteriol 177:723-732. https://doi.org/10.1128/jb.177.3.723-732.1995
    • (1995) J Bacteriol , vol.177 , pp. 723-732
    • Henrich, B.1    Binishofer, B.2    Bläsi, U.3
  • 32
    • 84901236282 scopus 로고    scopus 로고
    • Genetic dissection of T4 lysis
    • Moussa SH, Lawler JL, Young R. 2014. Genetic dissection of T4 lysis. J Bacteriol 196:2201-2209. https://doi.org/10.1128/JB.01548-14
    • (2014) J Bacteriol , vol.196 , pp. 2201-2209
    • Moussa, S.H.1    Lawler, J.L.2    Young, R.3
  • 33
    • 0033758762 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of dimer and oligomer interactions of the lambda S holin
    • Grundling A, Bläsi U, Young R. 2000. Genetic and biochemical analysis of dimer and oligomer interactions of the lambda S holin. J Bacteriol 182:6082-6090. https://doi.org/10.1128/JB.182.21.6082-6090.2000
    • (2000) J Bacteriol , vol.182 , pp. 6082-6090
    • Grundling, A.1    Bläsi, U.2    Young, R.3
  • 35
    • 84860484350 scopus 로고    scopus 로고
    • Fine tuning of the lactate and diacetyl production through promoter engineering in Lactococcus lactis
    • Guo T, Kong J, Zhang L, Zhang C, Hu S. 2012. Fine tuning of the lactate and diacetyl production through promoter engineering in Lactococcus lactis. PLoS One 7:e36296. https://doi.org/10.1371/journal.pone.0036296
    • (2012) PLoS One , vol.7
    • Guo, T.1    Kong, J.2    Zhang, L.3    Zhang, C.4    Hu, S.5
  • 36
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schägger H. 2006. Tricine-SDS-PAGE. Nat Protoc 1:16-22. https://doi .org/10.1038/nprot.2006.4
    • (2006) Nat Protoc , vol.1 , pp. 16-22
    • Schägger, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.