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Volumn 109, Issue 18, 2012, Pages 7073-7078

Bacteriophage T4 polynucleotide kinase triggers degradation of mRNAs

Author keywords

mRNA turnover; Viral cycle

Indexed keywords

EXONUCLEASE; MESSENGER RNA; PHOSPHATASE; POLYNUCLEOTIDE; RIBONUCLEASE;

EID: 84860830992     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1119802109     Document Type: Article
Times cited : (14)

References (41)
  • 1
    • 64049083937 scopus 로고    scopus 로고
    • RNA processing and decay in bacteriophage T4
    • Uzan M (2009) RNA processing and decay in bacteriophage T4. Prog Mol Biol Transl Sci 85:43-89.
    • (2009) Prog Mol Biol Transl Sci , vol.85 , pp. 43-89
    • Uzan, M.1
  • 2
    • 77955149193 scopus 로고    scopus 로고
    • The critical role of RNA processing and degradation in the control of gene expression
    • Arraiano CM, et al. (2010) The critical role of RNA processing and degradation in the control of gene expression. FEMS Microbiol Rev 34:883-923.
    • (2010) FEMS Microbiol Rev , vol.34 , pp. 883-923
    • Arraiano, C.M.1
  • 4
    • 0032531768 scopus 로고    scopus 로고
    • Ribonuclease E is a 5′-end-dependent endonuclease
    • Mackie GA (1998) Ribonuclease E is a 5′-end-dependent endonuclease. Nature 395: 720-723.
    • (1998) Nature , vol.395 , pp. 720-723
    • Mackie, G.A.1
  • 5
    • 0034708447 scopus 로고    scopus 로고
    • The CafA protein required for the 5'-maturation of 16 S rRNA is a 5'- end-dependent ribonuclease that has context-dependent broad sequence specificity
    • DOI 10.1074/jbc.275.12.8726
    • Tock MR, Walsh AP, Carroll G, McDowall KJ (2000) The CafA protein required for the 5′-maturation of 16 S rRNA is a 5′-end-dependent ribonuclease that has context-dependent broad sequence specificity. J Biol Chem 275:8726-8732. (Pubitemid 30180225)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.12 , pp. 8726-8732
    • Tock, M.R.1    Walsh, A.P.2    Carroll, G.3    McDowall, K.J.4
  • 6
    • 36849032886 scopus 로고    scopus 로고
    • Sensing of 5′ monophosphate by Escherichia coli RNase G can significantly enhance association with RNA and stimulate the decay of functional mRNA transcripts in vivo
    • DOI 10.1111/j.1365-2958.2007.06028.x
    • Jourdan SS, McDowall KJ (2008) Sensing of 5′ monophosphate by Escherichia coli RNase G can significantly enhance association with RNA and stimulate the decay of functional mRNA transcripts in vivo. Mol Microbiol 67:102-115. (Pubitemid 350231139)
    • (2008) Molecular Microbiology , vol.67 , Issue.1 , pp. 102-115
    • Jourdan, S.S.1    McDowall, K.J.2
  • 7
    • 38349117689 scopus 로고    scopus 로고
    • The bacterial enzyme RppH triggers messenger RNA degradation by 5′ pyrophosphate removal
    • Deana A, Celesnik H, Belasco JG (2008) The bacterial enzyme RppH triggers messenger RNA degradation by 5′ pyrophosphate removal. Nature 451:355-358.
    • (2008) Nature , vol.451 , pp. 355-358
    • Deana, A.1    Celesnik, H.2    Belasco, J.G.3
  • 8
    • 0024162978 scopus 로고
    • A nuclease that cuts specifically in the ribosome binding site of some T4 mRNAs
    • Uzan M, Favre R, Brody E (1988) A nuclease that cuts specifically in the ribosome binding site of some T4 mRNAs. Proc Natl Acad Sci USA 85:8895-8899.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8895-8899
    • Uzan, M.1    Favre, R.2    Brody, E.3
  • 9
    • 33845887686 scopus 로고    scopus 로고
    • Activation of RegB endoribonuclease by S1 ribosomal protein requires an 11 nt conserved sequence
    • DOI 10.1093/nar/gkl911
    • Durand S, et al. (2006) Activation of RegB endoribonuclease by S1 ribosomal protein requires an 11 nt conserved sequence. Nucleic Acids Res 34:6549-6560. (Pubitemid 46017950)
    • (2006) Nucleic Acids Research , vol.34 , Issue.22 , pp. 6549-6560
    • Durand, S.1    Richard, G.2    Bisaglia, M.3    Laalami, S.4    Bontems, F.5    Uzan, M.6
  • 10
    • 0027442208 scopus 로고
    • Dual role of the sequence-specific bacteriophage T4 endoribonuclease RegB. mRNA inactivation and mRNA destabilization
    • DOI 10.1006/jmbi.1993.1522
    • Sanson B, Uzan M (1993) Dual role of the sequence-specific bacteriophage T4 endoribonuclease RegB. mRNA inactivation and mRNA destabilization. J Mol Biol 233: 429-446. (Pubitemid 23299172)
    • (1993) Journal of Molecular Biology , vol.233 , Issue.3 , pp. 429-446
    • Sanson, B.1    Uzan, M.2
  • 11
    • 0034646557 scopus 로고    scopus 로고
    • Endoribonuclease RegB from bacteriophage T4 is necessary for the degradation of early but not middle or late mRNAs
    • Sanson B, Hu RM, Troitskaya E, Mathy N, Uzan M (2000) Endoribonuclease RegB from bacteriophage T4 is necessary for the degradation of early but not middle or late mRNAs. J Mol Biol 297:1063-1074.
    • (2000) J Mol Biol , vol.297 , pp. 1063-1074
    • Sanson, B.1    Hu, R.M.2    Troitskaya, E.3    Mathy, N.4    Uzan, M.5
  • 12
    • 0038606983 scopus 로고    scopus 로고
    • The phage T4 restriction endoribonuclease RegB: A cyclizing enzyme that requires two histidines to be fully active
    • DOI 10.1093/nar/gkg377
    • Saïda F, Uzan M, Bontems F (2003) The phage T4 restriction endoribonuclease RegB: A cyclizing enzyme that requires two histidines to be fully active. Nucleic Acids Res 31: 2751-2758. (Pubitemid 37442119)
    • (2003) Nucleic Acids Research , vol.31 , Issue.11 , pp. 2751-2758
    • Saida, F.1    Uzan, M.2    Bontems, F.3
  • 14
    • 0029128350 scopus 로고
    • Post-transcriptional controls in bacteriophage T4: Roles of the sequence-specific endoribonuclease RegB
    • Sanson B, Uzan M (1995) Post-transcriptional controls in bacteriophage T4: Roles of the sequence-specific endoribonuclease RegB. FEMS Microbiol Rev 17:141-150.
    • (1995) FEMS Microbiol Rev , vol.17 , pp. 141-150
    • Sanson, B.1    Uzan, M.2
  • 15
    • 43349107339 scopus 로고    scopus 로고
    • Involvement of the Escherichia coli endoribonucleases G and E in the secondary processing of RegB-cleaved transcripts of bacteriophage T4
    • Zajanckauskaite A, Truncaite L, Strazdaite-Zieliene Z, Nivinskas R (2008) Involvement of the Escherichia coli endoribonucleases G and E in the secondary processing of RegB-cleaved transcripts of bacteriophage T4. Virology 375:342-353.
    • (2008) Virology , vol.375 , pp. 342-353
    • Zajanckauskaite, A.1    Truncaite, L.2    Strazdaite-Zieliene, Z.3    Nivinskas, R.4
  • 16
    • 0023388202 scopus 로고
    • Bacteriophage T4 anticodon nuclease, polynucleotide kinase and RNA ligase reprocess the host lysine tRNA
    • Amitsur M, Levitz R, Kaufmann G (1987) Bacteriophage T4 anticodon nuclease, polynucleotide kinase and RNA ligase reprocess the host lysine tRNA. EMBO J 6: 2499-2503.
    • (1987) EMBO J , vol.6 , pp. 2499-2503
    • Amitsur, M.1    Levitz, R.2    Kaufmann, G.3
  • 17
    • 33745307149 scopus 로고    scopus 로고
    • PrrC-anticodon nuclease: Functional organization of a prototypical bacterial restriction RNase
    • Blanga-Kanfi S, Amitsur M, Azem A, Kaufmann G (2006) PrrC-anticodon nuclease: Functional organization of a prototypical bacterial restriction RNase. Nucleic Acids Res 34:3209-3219.
    • (2006) Nucleic Acids Res , vol.34 , pp. 3209-3219
    • Blanga-Kanfi, S.1    Amitsur, M.2    Azem, A.3    Kaufmann, G.4
  • 18
    • 0013791279 scopus 로고
    • Phosphorylation of nucleic acid by an enzyme from T4 bacteriophage- infected Escherichia coli
    • Richardson CC (1965) Phosphorylation of nucleic acid by an enzyme from T4 bacteriophage-infected Escherichia coli. Proc Natl Acad Sci USA 54:158-165.
    • (1965) Proc Natl Acad Sci USA , vol.54 , pp. 158-165
    • Richardson, C.C.1
  • 19
    • 0018098860 scopus 로고
    • A role in true-late gene expression for the T4 bacteriophage 5' polynucleotide kinase 3' phosphatase
    • Sirotkin K, Cooley W, Runnels J, Snyder LR (1978) A role in true-late gene expression for the T4 bacteriophage 5′ polynucleotide kinase 3′ phosphatase. J Mol Biol 123: 221-233. (Pubitemid 8406690)
    • (1978) Journal of Molecular Biology , vol.123 , Issue.2 , pp. 221-233
    • Sirotkin, K.1    Cooley, W.2    Runnels, J.3    Snyder, L.R.4
  • 20
    • 0017883477 scopus 로고
    • Polynucleotide kinase from a T4 mutant which lacks the 3' phosphatase activity
    • Cameron V, Soltis D, Uhlenbeck OC (1978) Polynucleotide kinase from a T4 mutant which lacks the 3′ phosphatase activity. Nucleic Acids Res 5:825-833. (Pubitemid 8291137)
    • (1978) Nucleic Acids Research , vol.5 , Issue.3 , pp. 825-833
    • Cameron, V.1    Soltis, D.2    Uhlenbeck, O.C.3
  • 21
    • 0034057267 scopus 로고    scopus 로고
    • The bacteriophage T4 anti-sigma factor AsiA is not necessary for the inhibition of early promoters in vivo
    • DOI 10.1046/j.1365-2958.2000.01787.x
    • Pène C, Uzan M (2000) The bacteriophage T4 anti-sigma factor AsiA is not necessary for the inhibition of early promoters in vivo. Mol Microbiol 35:1180-1191. (Pubitemid 30137786)
    • (2000) Molecular Microbiology , vol.35 , Issue.5 , pp. 1180-1191
    • Pene, C.1    Uzan, M.2
  • 23
    • 0026713274 scopus 로고
    • Sequence and characterization of the bacteriophage T4 comC alpha gene product, a possible transcription antitermination factor
    • Sanson B, Uzan M (1992) Sequence and characterization of the bacteriophage T4 comC alpha gene product, a possible transcription antitermination factor. J Bacteriol 174:6539-6547.
    • (1992) J Bacteriol , vol.174 , pp. 6539-6547
    • Sanson, B.1    Uzan, M.2
  • 24
    • 77958571327 scopus 로고    scopus 로고
    • Transcriptional control in the prereplicative phase of T4 development
    • Hinton DM (2010) Transcriptional control in the prereplicative phase of T4 development. Virol J 7:289.
    • (2010) Virol J , vol.7 , pp. 289
    • Hinton, D.M.1
  • 25
    • 70450222923 scopus 로고    scopus 로고
    • RNase Y, a novel endoribonuclease, initiates riboswitch turnover in Bacillus subtilis
    • Shahbabian K, Jamalli A, Zig L, Putzer H (2009) RNase Y, a novel endoribonuclease, initiates riboswitch turnover in Bacillus subtilis. EMBO J 28:3523-3533.
    • (2009) EMBO J , vol.28 , pp. 3523-3533
    • Shahbabian, K.1    Jamalli, A.2    Zig, L.3    Putzer, H.4
  • 27
    • 0018902741 scopus 로고
    • Purification and characterization of a Saccharomyces cerevisiae exoribonuclease which yields 5′-mononucleotides by a 5′ leads to 3′ mode of hydrolysis
    • Stevens A (1980) Purification and characterization of a Saccharomyces cerevisiae exoribonuclease which yields 5′-mononucleotides by a 5′ leads to 3′ mode of hydrolysis. J Biol Chem 255:3080-3085.
    • (1980) J Biol Chem , vol.255 , pp. 3080-3085
    • Stevens, A.1
  • 28
    • 0023163751 scopus 로고
    • A 5'′3' exoribonuclease of human placental nuclei: Purification and substrate specificity
    • Stevens A, Maupin MK (1987) A 5′ - 3′ exoribonuclease of human placental nuclei: Purification and substrate specificity. Nucleic Acids Res 15:695-708. (Pubitemid 17234000)
    • (1987) Nucleic Acids Research , vol.15 , Issue.2 , pp. 695-708
    • Stevens, A.1    Maupin, M.K.2
  • 29
    • 0029024239 scopus 로고
    • 5′-exonuclease-2 of Saccharomyces cerevisiae. Purification and features of ribonuclease activity with comparison to 5′-exonuclease-1
    • Stevens A, Poole TL (1995) 5′-exonuclease-2 of Saccharomyces cerevisiae. Purification and features of ribonuclease activity with comparison to 5′-exonuclease-1. J Biol Chem 270:16063-16069.
    • (1995) J Biol Chem , vol.270 , pp. 16063-16069
    • Stevens, A.1    Poole, T.L.2
  • 30
    • 71149112138 scopus 로고    scopus 로고
    • Rrp17p is a eukaryotic exonuclease required for 5′ end processing of Pre-60S ribosomal RNA
    • Oeffinger M, et al. (2009) Rrp17p is a eukaryotic exonuclease required for 5′ end processing of Pre-60S ribosomal RNA. Mol Cell 36:768-781.
    • (2009) Mol Cell , vol.36 , pp. 768-781
    • Oeffinger, M.1
  • 31
    • 80052988291 scopus 로고    scopus 로고
    • An RNA pyrophosphohydrolase triggers 5′-exonucleolytic degradation of mRNA in Bacillus subtilis
    • Richards J, et al. (2011) An RNA pyrophosphohydrolase triggers 5′-exonucleolytic degradation of mRNA in Bacillus subtilis. Mol Cell 43:940-949.
    • (2011) Mol Cell , vol.43 , pp. 940-949
    • Richards, J.1
  • 32
    • 64749111945 scopus 로고    scopus 로고
    • Structure and function of the 5′→3′ exoribonuclease Rat1 and its activating partner Rai1
    • Xiang S, et al. (2009) Structure and function of the 5′→ 3′ exoribonuclease Rat1 and its activating partner Rai1. Nature 458:784-788.
    • (2009) Nature , vol.458 , pp. 784-788
    • Xiang, S.1
  • 33
    • 78650285324 scopus 로고    scopus 로고
    • Nol9 is a novel polynucleotide 5′-kinase involved in ribosomal RNA processing
    • Heindl K, Martinez J (2010) Nol9 is a novel polynucleotide 5′-kinase involved in ribosomal RNA processing. EMBO J 29:4161-4171.
    • (2010) EMBO J , vol.29 , pp. 4161-4171
    • Heindl, K.1    Martinez, J.2
  • 34
    • 42149123284 scopus 로고    scopus 로고
    • Efficient termination of transcription by RNA polymerase I requires the 5′ exonuclease Rat1 in yeast
    • DOI 10.1101/gad.463708
    • El Hage A, Koper M, Kufel J, Tollervey D (2008) Efficient termination of transcription by RNA polymerase I requires the 5′ exonuclease Rat1 in yeast. Genes Dev 22: 1069-1081. (Pubitemid 351544244)
    • (2008) Genes and Development , vol.22 , Issue.8 , pp. 1069-1081
    • El, H.A.1    Koper, M.2    Kufel, J.3    Tollervey, D.4
  • 35
    • 77957223021 scopus 로고    scopus 로고
    • Role of the RNA/DNA kinase Grc3 in transcription termination by RNA polymerase I
    • Braglia P, Heindl K, Schleiffer A, Martinez J, Proudfoot NJ (2010) Role of the RNA/DNA kinase Grc3 in transcription termination by RNA polymerase I. EMBO Rep 11:758-764.
    • (2010) EMBO Rep , vol.11 , pp. 758-764
    • Braglia, P.1    Heindl, K.2    Schleiffer, A.3    Martinez, J.4    Proudfoot, N.J.5
  • 36
    • 0016378791 scopus 로고
    • Genetics and physiology of bacteriophage T4 3′-phosphatase: Evidence for involvement of the enzyme in T4 DNA metabolism
    • Depew RE, Cozzarelli NR (1974) Genetics and physiology of bacteriophage T4 3′-phosphatase: Evidence for involvement of the enzyme in T4 DNA metabolism. J Virol 13:888-897.
    • (1974) J Virol , vol.13 , pp. 888-897
    • Depew, R.E.1    Cozzarelli, N.R.2
  • 37
    • 0035018365 scopus 로고    scopus 로고
    • Involvement of RNase G in in vivo mRNA metabolism in Escherichia coli
    • DOI 10.1046/j.1365-2443.2001.00430.x
    • Umitsuki G, Wachi M, Takada A, Hikichi T, Nagai K (2001) Involvement of RNase G in in vivo mRNA metabolism in Escherichia coli. Genes Cells 6:403-410. (Pubitemid 32487451)
    • (2001) Genes to Cells , vol.6 , Issue.5 , pp. 403-410
    • Umitsuki, G.1    Wachi, M.2    Takada, A.3    Hikichi, T.4    Nagai, K.5
  • 38
    • 0031020242 scopus 로고    scopus 로고
    • Functional relationship between Escherichia coli RNase E and the CafA protein
    • Wachi M, Umitsuki G, Nagai K (1997) Functional relationship between Escherichia coli RNase E and the CafA protein. Mol Gen Genet 253:515-519.
    • (1997) Mol Gen Genet , vol.253 , pp. 515-519
    • Wachi, M.1    Umitsuki, G.2    Nagai, K.3


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