메뉴 건너뛰기




Volumn 398, Issue 1, 2010, Pages 38-43

APOBEC-1 complementation factor (ACF) forms RNA-dependent multimers

Author keywords

ACF; APOBEC 1; APOBEC 1 complementation factor; Apolipoprotein B; Editosome; MRNA editing

Indexed keywords

APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 1; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 1 COMPLEMENTATION FACTOR; CYTOSINE; MESSENGER RNA; RNA BINDING PROTEIN; UNCLASSIFIED DRUG; URACIL;

EID: 77954759537     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.06.021     Document Type: Article
Times cited : (11)

References (35)
  • 1
    • 0034733528 scopus 로고    scopus 로고
    • Purification and molecular cloning of a novel essential component of the apolipoprotein B mRNA editing enzyme-complex
    • Lellek H., Kirsten R., Diehl I., Apostel F., Buck F., Greeve J. Purification and molecular cloning of a novel essential component of the apolipoprotein B mRNA editing enzyme-complex. J. Biol. Chem. 2000, 275:19848-19856.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19848-19856
    • Lellek, H.1    Kirsten, R.2    Diehl, I.3    Apostel, F.4    Buck, F.5    Greeve, J.6
  • 2
    • 0033970066 scopus 로고    scopus 로고
    • Molecular cloning of apobec-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA
    • Mehta A., Kinter M.T., Sherman N.E., Driscoll D.M. Molecular cloning of apobec-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA. Mol. Cell. Biol. 2000, 20:1846-1854.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1846-1854
    • Mehta, A.1    Kinter, M.T.2    Sherman, N.E.3    Driscoll, D.M.4
  • 3
    • 18544377013 scopus 로고    scopus 로고
    • The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression
    • Maris C., Dominguez C., Allain F.H. The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression. FEBS J. 2005, 272:2118-2131.
    • (2005) FEBS J. , vol.272 , pp. 2118-2131
    • Maris, C.1    Dominguez, C.2    Allain, F.H.3
  • 4
    • 0027651240 scopus 로고
    • Apolipoprotein B mRNA editing: the sequence to the event
    • Smith H.C. Apolipoprotein B mRNA editing: the sequence to the event. Semin. Cell Biol. 1993, 4:267-278.
    • (1993) Semin. Cell Biol. , vol.4 , pp. 267-278
    • Smith, H.C.1
  • 5
    • 12844281639 scopus 로고    scopus 로고
    • NMR structure of the apoB mRNA stem-loop and its interaction with the C to U editing APOBEC1 complementary factor
    • Maris C., Masse J., Chester A., Navaratnam N., Allain F.H. NMR structure of the apoB mRNA stem-loop and its interaction with the C to U editing APOBEC1 complementary factor. RNA 2005, 11:173-186.
    • (2005) RNA , vol.11 , pp. 173-186
    • Maris, C.1    Masse, J.2    Chester, A.3    Navaratnam, N.4    Allain, F.H.5
  • 7
    • 0037107401 scopus 로고    scopus 로고
    • Large-scale induced fit recognition of an m(7)GpppG cap analogue by the human nuclear cap-binding complex
    • Mazza C., Segref A., Mattaj I.W., Cusack S. Large-scale induced fit recognition of an m(7)GpppG cap analogue by the human nuclear cap-binding complex. Embo J. 2002, 21:5548-5557.
    • (2002) Embo J. , vol.21 , pp. 5548-5557
    • Mazza, C.1    Segref, A.2    Mattaj, I.W.3    Cusack, S.4
  • 8
    • 1642348680 scopus 로고    scopus 로고
    • Solution structure of the complex formed by the two N-terminal RNA-binding domains of nucleolin and a pre-rRNA target
    • Johansson C., Finger L.D., Trantirek L., Mueller T.D., Kim S., Laird-Offringa I.A., Feigon J. Solution structure of the complex formed by the two N-terminal RNA-binding domains of nucleolin and a pre-rRNA target. J. Mol. Biol. 2004, 337:799-816.
    • (2004) J. Mol. Biol. , vol.337 , pp. 799-816
    • Johansson, C.1    Finger, L.D.2    Trantirek, L.3    Mueller, T.D.4    Kim, S.5    Laird-Offringa, I.A.6    Feigon, J.7
  • 9
    • 0036202559 scopus 로고    scopus 로고
    • Identification of Domains in APOBEC-1 complementation factor required for RNA binding and apolipoprotein B mRNA editing
    • Mehta A., Driscoll D.M. Identification of Domains in APOBEC-1 complementation factor required for RNA binding and apolipoprotein B mRNA editing. RNA 2002, 8:69-82.
    • (2002) RNA , vol.8 , pp. 69-82
    • Mehta, A.1    Driscoll, D.M.2
  • 10
    • 0035824516 scopus 로고    scopus 로고
    • Mutagenesis of apobec-1 complementation factor reveals distinct domains that modulate RNA binding, protein-protein interaction with apobec-1, and complementation of C to U RNA-editing activity
    • Blanc V., Henderson J.O., Kennedy S., Davidson N.O. Mutagenesis of apobec-1 complementation factor reveals distinct domains that modulate RNA binding, protein-protein interaction with apobec-1, and complementation of C to U RNA-editing activity. J. Biol. Chem. 2001, 276:46386-46393.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46386-46393
    • Blanc, V.1    Henderson, J.O.2    Kennedy, S.3    Davidson, N.O.4
  • 12
    • 33746281453 scopus 로고    scopus 로고
    • Metabolic regulation of apoB mRNA editing is associated with phosphorylation of APOBEC-1 complementation factor
    • Lehmann D.M., Galloway C.A., Sowden M.P., Smith H.C. Metabolic regulation of apoB mRNA editing is associated with phosphorylation of APOBEC-1 complementation factor. Nucleic Acids Res. 2006, 34:3299-3308.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 3299-3308
    • Lehmann, D.M.1    Galloway, C.A.2    Sowden, M.P.3    Smith, H.C.4
  • 13
    • 0142135078 scopus 로고    scopus 로고
    • A novel nuclear localization signal in the auxiliary domain of apobec-1 complementation factor regulates nucleocytoplasmic import and shuttling
    • Blanc V., Kennedy S., Davidson N.O. A novel nuclear localization signal in the auxiliary domain of apobec-1 complementation factor regulates nucleocytoplasmic import and shuttling. J. Biol. Chem. 2003, 278:41198-41204.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41198-41204
    • Blanc, V.1    Kennedy, S.2    Davidson, N.O.3
  • 14
    • 0347052885 scopus 로고    scopus 로고
    • Identification of novel alternative splice variants of APOBEC-1 complementation factor with different capacities to support ApoB mRNA editing
    • Sowden M.P., Lehmann D.M., Lin X., Smith C.O., Smith H.C. Identification of novel alternative splice variants of APOBEC-1 complementation factor with different capacities to support ApoB mRNA editing. J. Biol. Chem. 2004, 278:197-206.
    • (2004) J. Biol. Chem. , vol.278 , pp. 197-206
    • Sowden, M.P.1    Lehmann, D.M.2    Lin, X.3    Smith, C.O.4    Smith, H.C.5
  • 15
    • 0037338060 scopus 로고    scopus 로고
    • Increasing the yield of soluble recombinant protein expressed in E. coli by induction during late log phase
    • (528, 530)
    • Galloway C.A., Sowden M.P., Smith H.C. Increasing the yield of soluble recombinant protein expressed in E. coli by induction during late log phase. BioTechniques 2003, 34:524-526. (528, 530).
    • (2003) BioTechniques , vol.34 , pp. 524-526
    • Galloway, C.A.1    Sowden, M.P.2    Smith, H.C.3
  • 16
    • 33645233077 scopus 로고    scopus 로고
    • A dark yellow fluorescent protein (YFP)-based resonance energy-accepting chromoprotein (REACh) for Forster resonance energy transfer with GFP
    • Ganesan S., Ameer-Beg S.M., Ng T.T., Vojnovic B., Wouters F.S. A dark yellow fluorescent protein (YFP)-based resonance energy-accepting chromoprotein (REACh) for Forster resonance energy transfer with GFP. Proc. Natl. Acad. Sci. USA 2006, 103:4089-4094.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 4089-4094
    • Ganesan, S.1    Ameer-Beg, S.M.2    Ng, T.T.3    Vojnovic, B.4    Wouters, F.S.5
  • 18
    • 0031694734 scopus 로고    scopus 로고
    • Analysis of protein complexes assembled on apolipoprotein B mRNA for mooring sequence-dependent RNA editing
    • Smith H.C. Analysis of protein complexes assembled on apolipoprotein B mRNA for mooring sequence-dependent RNA editing. Methods 1998, 15:27-39.
    • (1998) Methods , vol.15 , pp. 27-39
    • Smith, H.C.1
  • 19
    • 0029805089 scopus 로고    scopus 로고
    • Determinants involved in regulating the proportion of edited apolipoprotein B RNAs
    • Sowden M., Hamm J.K., Spinelli S., Smith H.C. Determinants involved in regulating the proportion of edited apolipoprotein B RNAs. RNA 1996, 2:274-288.
    • (1996) RNA , vol.2 , pp. 274-288
    • Sowden, M.1    Hamm, J.K.2    Spinelli, S.3    Smith, H.C.4
  • 20
    • 0034654352 scopus 로고    scopus 로고
    • A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions
    • Philo J.S. A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions. Anal. Biochem. 2000, 279:151-163.
    • (2000) Anal. Biochem. , vol.279 , pp. 151-163
    • Philo, J.S.1
  • 21
    • 33745216899 scopus 로고    scopus 로고
    • Improved methods for fitting sedimentation coefficient distributions derived by time-derivative techniques
    • Philo J.S. Improved methods for fitting sedimentation coefficient distributions derived by time-derivative techniques. Anal. Biochem. 2006, 354:238-246.
    • (2006) Anal. Biochem. , vol.354 , pp. 238-246
    • Philo, J.S.1
  • 22
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck P. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys. J. 2000, 78:1606-1619.
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 23
    • 0036500884 scopus 로고    scopus 로고
    • The editosome for cytidine to uridine mRNA editing has a native complexity of 27S: identification of intracellular domains containing active and inactive editing factors
    • Sowden M.P., Ballatori N., de Mesy Jensen K.L., Hamilton Reed L., Smith H.C. The editosome for cytidine to uridine mRNA editing has a native complexity of 27S: identification of intracellular domains containing active and inactive editing factors. J. Cell Sci. 2002, 115:1027-1039.
    • (2002) J. Cell Sci. , vol.115 , pp. 1027-1039
    • Sowden, M.P.1    Ballatori, N.2    de Mesy Jensen, K.L.3    Hamilton Reed, L.4    Smith, H.C.5
  • 24
    • 0035153840 scopus 로고    scopus 로고
    • Structural basis for recognition of AU-rich element RNA by the HuD protein
    • Wang X., Tanaka Hall T.M. Structural basis for recognition of AU-rich element RNA by the HuD protein. Nat. Struct. Biol. 2001, 8:141-145.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 141-145
    • Wang, X.1    Tanaka Hall, T.M.2
  • 25
    • 0033578927 scopus 로고    scopus 로고
    • Recognition of polyadenylate RNA by the poly(A)-binding protein
    • Deo R.C., Bonanno J.B., Sonenberg N., Burley S.K. Recognition of polyadenylate RNA by the poly(A)-binding protein. Cell 1999, 98:835-845.
    • (1999) Cell , vol.98 , pp. 835-845
    • Deo, R.C.1    Bonanno, J.B.2    Sonenberg, N.3    Burley, S.K.4
  • 27
    • 0027450461 scopus 로고
    • Extract-specific heterogeneity in high-order complexes containing apolipoprotein B mRNA editing activity and RNA-binding proteins
    • Harris S.G., Sabio I., Mayer E., Steinberg M.F., Backus J.W., Sparks J.D., Sparks C.E., Smith H.C. Extract-specific heterogeneity in high-order complexes containing apolipoprotein B mRNA editing activity and RNA-binding proteins. J. Biol. Chem. 1993, 268:7382-7392.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7382-7392
    • Harris, S.G.1    Sabio, I.2    Mayer, E.3    Steinberg, M.F.4    Backus, J.W.5    Sparks, J.D.6    Sparks, C.E.7    Smith, H.C.8
  • 28
    • 4644318881 scopus 로고    scopus 로고
    • Gene structure and expression of the mouse APOBEC-1 complementation factor: multiple transcriptional initiation sites and a spliced variant with a premature stop translation codon
    • Dur S., Krause K., Pluntke N., Greeve J. Gene structure and expression of the mouse APOBEC-1 complementation factor: multiple transcriptional initiation sites and a spliced variant with a premature stop translation codon. Biochim. Biophys. Acta 2004, 1680:11-23.
    • (2004) Biochim. Biophys. Acta , vol.1680 , pp. 11-23
    • Dur, S.1    Krause, K.2    Pluntke, N.3    Greeve, J.4
  • 29
    • 0035846449 scopus 로고    scopus 로고
    • Isolation, characterization and developmental regulation of the human apobec-1 complementation factor (ACF) gene
    • Henderson J.O., Blanc V., Davidson N.O. Isolation, characterization and developmental regulation of the human apobec-1 complementation factor (ACF) gene. Biochim. Biophys. Acta 2001, 1522:22-30.
    • (2001) Biochim. Biophys. Acta , vol.1522 , pp. 22-30
    • Henderson, J.O.1    Blanc, V.2    Davidson, N.O.3
  • 31
    • 57749083751 scopus 로고    scopus 로고
    • Measuring editing activity and identifying cytidine-to-uridine mRNA editing factors in cells and biochemical isolates
    • Smith H.C. Measuring editing activity and identifying cytidine-to-uridine mRNA editing factors in cells and biochemical isolates. Methods Enzymol. 2007, 424:389-416.
    • (2007) Methods Enzymol. , vol.424 , pp. 389-416
    • Smith, H.C.1
  • 32
    • 0034070741 scopus 로고    scopus 로고
    • The NMR structure of the 38kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein
    • Varani L., Gunderson S.I., Mattaj I.W., Kay L.E., Neuhaus D., Varani G. The NMR structure of the 38kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein. Nat. Struct. Biol. 2000, 7:329-335.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 329-335
    • Varani, L.1    Gunderson, S.I.2    Mattaj, I.W.3    Kay, L.E.4    Neuhaus, D.5    Varani, G.6
  • 33
    • 0028085932 scopus 로고
    • Dimeric structure of a human apo B mRNA editing protein and cloning and chromosomal localization of its gene
    • Lau P.P., Zhu H.-J., Baldini A., Charnsangavej C., Chan L. Dimeric structure of a human apo B mRNA editing protein and cloning and chromosomal localization of its gene. Proc. Natl. Acad. Sci. USA 1994, 91:8522-8526.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8522-8526
    • Lau, P.P.1    Zhu, H.-J.2    Baldini, A.3    Charnsangavej, C.4    Chan, L.5
  • 34
    • 0032958220 scopus 로고    scopus 로고
    • Mutational analysis of apolipoprotein B mRNA editing enzyme (APOBEC1). Structure-function relationships of RNA editing and dimerization
    • Teng B.B., Ochsner S., Zhang Q., Soman K.V., Lau P.P., Chan L. Mutational analysis of apolipoprotein B mRNA editing enzyme (APOBEC1). Structure-function relationships of RNA editing and dimerization. J. Lipid Res. 1999, 40:623-635.
    • (1999) J. Lipid Res. , vol.40 , pp. 623-635
    • Teng, B.B.1    Ochsner, S.2    Zhang, Q.3    Soman, K.V.4    Lau, P.P.5    Chan, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.