메뉴 건너뛰기




Volumn 31, Issue 15, 2003, Pages 4317-4325

Divalent metal-dependent catalysis and cleavage specificity of CSP41, a chloroplast endoribonuclease belonging to the short chain dehydrogenase/reductase superfamily

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOTENSIN; ASPARAGINE; CALCIUM CHLORIDE; CALCIUM ION; CHLOROPLAST RNA; COPPER ION; DOUBLE STRANDED RNA; ENDONUCLEASE; MAGNESIUM CHLORIDE; MAGNESIUM ION; MANGANESE; METAL; OXIDOREDUCTASE; RNA BINDING PROTEIN; ZINC ION; CALCIUM; CYTOCHROME B; CYTOCHROME B6F; DIVALENT CATION; ENDORIBONUCLEASE CSP41; MAGNESIUM; PETD PROTEIN, CYTOCHROME B(6)F COMPLEX; PLANT RNA; RIBONUCLEASE;

EID: 0043163808     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkg640     Document Type: Article
Times cited : (23)

References (38)
  • 1
    • 0024962578 scopus 로고
    • Function of plastid mRNA 3′ inverted repeats: RNA stabilization and gene-specific protein binding
    • Stern,D.B., Jones,H. and Gruissem,W. (1989) Function of plastid mRNA 3′ inverted repeats: RNA stabilization and gene-specific protein binding. J. Biol. Chem., 264, 18742-18750.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18742-18750
    • Stern, D.B.1    Jones, H.2    Gruissem, W.3
  • 2
    • 0025784440 scopus 로고
    • Specific binding of chloroplast proteins in vitro to the 3′ untranslated region of spinach chloroplast petD messenger RNA
    • Chen,H.C. and Stern,D.B. (1991) Specific binding of chloroplast proteins in vitro to the 3′ untranslated region of spinach chloroplast petD messenger RNA. Mol. Cell. Biol., 11, 4380-4388.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4380-4388
    • Chen, H.C.1    Stern, D.B.2
  • 3
    • 0030108651 scopus 로고    scopus 로고
    • RNA-binding proteins of 37/38 kDa bind specifically to the barley chloroplast psbA 3′-end untranslated RNA
    • Memon,A.R., Meng,B. and Mullet,J.E. (1996) RNA-binding proteins of 37/38 kDa bind specifically to the barley chloroplast psbA 3′-end untranslated RNA. Plant Mol. Biol., 30, 1195-1205.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 1195-1205
    • Memon, A.R.1    Meng, B.2    Mullet, J.E.3
  • 4
    • 0033861250 scopus 로고    scopus 로고
    • Processing and degradation of chloroplast mRNA
    • Monde,R.A., Schuster,G. and Stern,D.B. (2000) Processing and degradation of chloroplast mRNA. Biochimie, 82, 573-582.
    • (2000) Biochimie , vol.82 , pp. 573-582
    • Monde, R.A.1    Schuster, G.2    Stern, D.B.3
  • 5
    • 0028971144 scopus 로고
    • mRNA decay in spinach chloroplasts: psbA mRNA degradation is initiated by endonucleolytic cleavages within the coding region
    • Klaff,P. (1995) mRNA decay in spinach chloroplasts: psbA mRNA degradation is initiated by endonucleolytic cleavages within the coding region. Nucleic Acids Res., 23, 4885-4892.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4885-4892
    • Klaff, P.1
  • 6
    • 0030468099 scopus 로고    scopus 로고
    • Polyadenylation accelerates degradation of chloroplast mRNA
    • Kudla,J., Hayes,R. and Gruissem,W. (1996) Polyadenylation accelerates degradation of chloroplast mRNA. EMBO J., 15, 7137-7146.
    • (1996) EMBO J. , vol.15 , pp. 7137-7146
    • Kudla, J.1    Hayes, R.2    Gruissem, W.3
  • 7
    • 0026344374 scopus 로고
    • Specific ribonuclease activities in spinach chloroplasts promote mRNA maturation and degradation
    • Chen,H. and Stern,D.B. (1991) Specific ribonuclease activities in spinach chloroplasts promote mRNA maturation and degradation. J. Biol. Chem., 266, 24205-24211.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24205-24211
    • Chen, H.1    Stern, D.B.2
  • 8
    • 0027582419 scopus 로고
    • The 54 kDa RNA-binding protein from mustard chloroplasts mediates endonucleolytic transcript 3′ end formation in vitro
    • Nickelsen,J. and Link,G. (1993) The 54 kDa RNA-binding protein from mustard chloroplasts mediates endonucleolytic transcript 3′ end formation in vitro. Plant J., 3, 537-544.
    • (1993) Plant J. , vol.3 , pp. 537-544
    • Nickelsen, J.1    Link, G.2
  • 9
    • 0030221344 scopus 로고    scopus 로고
    • CSP41, a sequence-specific chloroplast mRNA binding protein, is an endoribonuclease
    • Yang,J., Schuster,G. and Stern,D.B. (1996) CSP41, a sequence-specific chloroplast mRNA binding protein, is an endoribonuclease. Plant Cell, 8, 1409-1420.
    • (1996) Plant Cell , vol.8 , pp. 1409-1420
    • Yang, J.1    Schuster, G.2    Stern, D.B.3
  • 10
    • 0031007946 scopus 로고    scopus 로고
    • The spinach chloroplast endoribonuclease CSP41 cleaves the 3′ untranslated region of petD mRNA primarily within its terminal stem-loop structure
    • Yang,J. and Stern,D.B. (1997) The spinach chloroplast endoribonuclease CSP41 cleaves the 3′ untranslated region of petD mRNA primarily within its terminal stem-loop structure. J. Biol. Chem., 272, 12784-12880.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12784-12880
    • Yang, J.1    Stern, D.B.2
  • 11
    • 0032551718 scopus 로고    scopus 로고
    • Spinach CSP41, an mRNA-binding protein and ribonuclease, is homologous to nucleotide-sugar epimerases and hydroxysteriod dehydrogenases
    • Baker,M.E., Grundy,W.N. and Elkan,C.P. (1998) Spinach CSP41, an mRNA-binding protein and ribonuclease, is homologous to nucleotide-sugar epimerases and hydroxysteriod dehydrogenases. Biochem. Biophys. Res. Commun., 248, 250-254.
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 250-254
    • Baker, M.E.1    Grundy, W.N.2    Elkan, C.P.3
  • 12
    • 0037493295 scopus 로고    scopus 로고
    • Secondary structures common to chloroplast mRNA 3′ UTRs direct cleavage by CSP41, an endoribonuclease belonging to the short chain dehydrogenase/reductase superfamily
    • in press
    • Bollenbach,T.J. and Stern,D.B. (2003) Secondary structures common to chloroplast mRNA 3′ UTRs direct cleavage by CSP41, an endoribonuclease belonging to the short chain dehydrogenase/reductase superfamily. J. Biol. Chem., 278, in press.
    • (2003) J. Biol. Chem. , vol.278
    • Bollenbach, T.J.1    Stern, D.B.2
  • 13
    • 2242454128 scopus 로고    scopus 로고
    • Dehydrogenases from all three domains of life cleave RNA
    • Evguenieva-Hackenberg,E., Schiltz,E. and Klug,G. (2002) Dehydrogenases from all three domains of life cleave RNA. J. Biol. Chem., 277, 46145-46150.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46145-46150
    • Evguenieva-Hackenberg, E.1    Schiltz, E.2    Klug, G.3
  • 15
    • 0027245417 scopus 로고
    • Novel ion specificity of a carboxylate cluster Mg(II) binding site: Strong charge selectivity and weak size selectivity
    • Needham,J.V., Chen,T.Y. and Falke,J.J. (1993) Novel ion specificity of a carboxylate cluster Mg(II) binding site: strong charge selectivity and weak size selectivity. Biochemistry, 32, 3363-3367.
    • (1993) Biochemistry , vol.32 , pp. 3363-3367
    • Needham, J.V.1    Chen, T.Y.2    Falke, J.J.3
  • 16
    • 0034634663 scopus 로고    scopus 로고
    • Gene-specific trans-regulatory functions of magnesium for chloroplast mRNA stability in higher plants
    • Horlitz,M. and Klaff,P. (2000) Gene-specific trans-regulatory functions of magnesium for chloroplast mRNA stability in higher plants. J. Biol. Chem., 275, 35638-35645.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35638-35645
    • Horlitz, M.1    Klaff, P.2
  • 18
    • 0023663880 scopus 로고
    • Control of plastid gene expression: 3′ inverted repeats act as mRNA processing and stabilizing elements, but do not terminate transcription
    • Stern,D.B. and Gruissem,W. (1987) Control of plastid gene expression: 3′ inverted repeats act as mRNA processing and stabilizing elements, but do not terminate transcription. Cell, 51, 1145-1157.
    • (1987) Cell , vol.51 , pp. 1145-1157
    • Stern, D.B.1    Gruissem, W.2
  • 19
    • 0033591465 scopus 로고    scopus 로고
    • Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure
    • Mathews,D.H., Sabina,J., Zuker,M. and Turner,D.H. (1999) Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure. J. Mol. Biol., 288, 911-940.
    • (1999) J. Mol. Biol. , vol.288 , pp. 911-940
    • Mathews, D.H.1    Sabina, J.2    Zuker, M.3    Turner, D.H.4
  • 20
    • 0026569967 scopus 로고
    • Cloning and domain structure of the mammalian splicing factor U2AF
    • Zamore,P.D., Patton,J.G. and Green,M.R. (1992) Cloning and domain structure of the mammalian splicing factor U2AF. Nature, 355, 609-614.
    • (1992) Nature , vol.355 , pp. 609-614
    • Zamore, P.D.1    Patton, J.G.2    Green, M.R.3
  • 21
    • 0026086816 scopus 로고
    • protein and through interactions with U2 snRNP-A′ protein
    • protein and through interactions with U2 snRNP-A′ protein. Mol. Cell. Biol., 11, 1829-1839.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1829-1839
    • Bentley, R.C.1    Keene, J.D.2
  • 22
    • 0034726714 scopus 로고    scopus 로고
    • Identification of the NAD(+)-binding fold of glyceraldehyde-3-phosphate dehydrogenase as a novel RNA-binding domain
    • Nagy,E., Henics,T., Eckert,M., Miseta,A., Lightowlers,R.N. and Kellermayer,M. (2000) Identification of the NAD(+)-binding fold of glyceraldehyde-3-phosphate dehydrogenase as a novel RNA-binding domain. Biochem. Biophys. Res. Commun., 275, 253-260.
    • (2000) Biochem. Biophys. Res. Commun. , vol.275 , pp. 253-260
    • Nagy, E.1    Henics, T.2    Eckert, M.3    Miseta, A.4    Lightowlers, R.N.5    Kellermayer, M.6
  • 23
    • 0021967957 scopus 로고
    • E.coli RNases: Making sense of alphabet soup
    • Deutscher,M.P. (1985) E.coli RNases: making sense of alphabet soup. Cell, 40, 731-732.
    • (1985) Cell , vol.40 , pp. 731-732
    • Deutscher, M.P.1
  • 24
    • 0027191132 scopus 로고
    • Ribonuclease III cleavage of a bacteriophage T7 processing signal. Divalent cation specificity and specific anion effects
    • Li,H.L., Chelladurai,B.S., Zhang,K. and Nicholson,A.W. (1993) Ribonuclease III cleavage of a bacteriophage T7 processing signal. Divalent cation specificity and specific anion effects. Nucleic Acids Res., 21, 1919-1925.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1919-1925
    • Li, H.L.1    Chelladurai, B.S.2    Zhang, K.3    Nicholson, A.W.4
  • 25
    • 0032545251 scopus 로고    scopus 로고
    • Activation/attenuation model for RNase H. A one-metal, mechanism with second-metal inhibition
    • Keck,J.L., Goedken,E.R. and Marqusee,S. (1998) Activation/attenuation model for RNase H. A one-metal, mechanism with second-metal inhibition. J. Biol. Chem., 273, 34128-34133.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34128-34133
    • Keck, J.L.1    Goedken, E.R.2    Marqusee, S.3
  • 26
    • 0034805756 scopus 로고    scopus 로고
    • Archaeoglobus fulgidus RNase HII in DNA replication: Enzymological functions and activity regulation via metal cofactors
    • Chai,Q., Qiu,J., Chapados,B.R. and Shen,B. (2001) Archaeoglobus fulgidus RNase HII in DNA replication: enzymological functions and activity regulation via metal cofactors. Biochem. Biophys. Res. Commun., 286, 1073-1081.
    • (2001) Biochem. Biophys. Res. Commun. , vol.286 , pp. 1073-1081
    • Chai, Q.1    Qiu, J.2    Chapados, B.R.3    Shen, B.4
  • 27
    • 0030972187 scopus 로고    scopus 로고
    • ARD-1 cDNA from human cells encodes a site-specific single-strand endoribonuclease that functionally resembles Escherichia coli RNase E
    • Claverie-Martin,F., Wang,M. and Cohen,S.N. (1997) ARD-1 cDNA from human cells encodes a site-specific single-strand endoribonuclease that functionally resembles Escherichia coli RNase E. J. Biol. Chem., 272, 13823-13828.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13823-13828
    • Claverie-Martin, F.1    Wang, M.2    Cohen, S.N.3
  • 28
    • 0020625791 scopus 로고
    • 7 S RNA: A single site substrate for the RNA processing enzyme ribonuclease E of Escherichia coli
    • Szeberenyi,J., Roy,M.K. and Apirion,D. (1983) 7 S RNA: a single site substrate for the RNA processing enzyme ribonuclease E of Escherichia coli. Biochim. Biophys. Acta, 740, 282-290.
    • (1983) Biochim. Biophys. Acta , vol.740 , pp. 282-290
    • Szeberenyi, J.1    Roy, M.K.2    Apirion, D.3
  • 29
    • 0036294225 scopus 로고    scopus 로고
    • Pre-steady-state and stopped-flow fluorescence analysis of Escherichia coli ribonuclease III: Insights into mechanism and conformational changes associated with binding and catalysis
    • Campbell,F.E.,Jr, Cassano,A.G., Anderson,V.E. and Harris,M.E. (2002) Pre-steady-state and stopped-flow fluorescence analysis of Escherichia coli ribonuclease III: insights into mechanism and conformational changes associated with binding and catalysis. J. Mol. Biol., 317, 21-40.
    • (2002) J. Mol. Biol. , vol.317 , pp. 21-40
    • Campbell, F.E.1    Cassano, A.G.2    Anderson, V.E.3    Harris, M.E.4
  • 30
    • 0035831544 scopus 로고    scopus 로고
    • 2+ ions reveals two divalent metals bound in the active site
    • 2+ ions reveals two divalent metals bound in the active site. J. Biol. Chem., 276, 7266-7271.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7266-7271
    • Goedken, E.R.1    Marqusee, S.2
  • 33
    • 0027249769 scopus 로고
    • Mutational analysis of a ribonuclease III processing signal
    • Chelladurai,B., Li,H., Zhang,K. and Nicholson,A.W. (1993) Mutational analysis of a ribonuclease III processing signal. Biochemistry, 32, 7549-7558.
    • (1993) Biochemistry , vol.32 , pp. 7549-7558
    • Chelladurai, B.1    Li, H.2    Zhang, K.3    Nicholson, A.W.4
  • 34
    • 0034692882 scopus 로고    scopus 로고
    • Towards understanding a molecular switch mechanism: Thermodynamic and crystallographic studies of the signal transduction protein CheY
    • Sola,M., Lopez-Hernandez,E., Cronet,P., Lacroix,E., Serrano,L., Coll,M. and Parraga,A. (2000) Towards understanding a molecular switch mechanism: thermodynamic and crystallographic studies of the signal transduction protein CheY. J. Mol. Biol., 303, 213-225.
    • (2000) J. Mol. Biol. , vol.303 , pp. 213-225
    • Sola, M.1    Lopez-Hernandez, E.2    Cronet, P.3    Lacroix, E.4    Serrano, L.5    Coll, M.6    Parraga, A.7
  • 35
    • 0034527837 scopus 로고    scopus 로고
    • The sequence and secondary structure of the 3′-UTR affect 3′-end maturation, RNA accumulation and translation in tobacco chloroplasts
    • Monde,R.A., Greene,J.C. and Stern,D.B. (2000) The sequence and secondary structure of the 3′-UTR affect 3′-end maturation, RNA accumulation and translation in tobacco chloroplasts. Plant Mol. Biol., 44, 529-542.
    • (2000) Plant Mol. Biol. , vol.44 , pp. 529-542
    • Monde, R.A.1    Greene, J.C.2    Stern, D.B.3
  • 38
    • 0023776628 scopus 로고
    • 2+-dependent chloroplast inorganic pyrophosphatase from Sorghum vulgare leaves
    • 2+-dependent chloroplast inorganic pyrophosphatase from Sorghum vulgare leaves. Arch. Biochem. Biophys., 260, 277-284.
    • (1988) Arch. Biochem. Biophys. , vol.260 , pp. 277-284
    • Krishnan, V.A.1    Gnanam, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.