메뉴 건너뛰기




Volumn 282, Issue 4, 1998, Pages 751-759

Isolation and physical characterization of random insertions in staphylococcal nuclease

Author keywords

Evolution; Genetic engineering; Internal duplication; Protein structure; Staphylococcal nuclease

Indexed keywords

GUANIDINE; NUCLEASE;

EID: 0032475838     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2063     Document Type: Article
Times cited : (8)

References (57)
  • 1
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • Andrade M.A., Chacón P., Morán F. Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng. 6:1993;383-390
    • (1993) Protein Eng. , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacón, P.2    Morán, F.3
  • 2
    • 0010657836 scopus 로고
    • Two-codon insertion mutagenesis of plasmid genes by using single-stranded hexameric oligonucleatides
    • Barany F. Two-codon insertion mutagenesis of plasmid genes by using single-stranded hexameric oligonucleatides. Proc. Natl Acad. Sci. USA. 82:1985;4202-4206
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 4202-4206
    • Barany, F.1
  • 3
    • 0028968250 scopus 로고
    • Energetics of denaturation and m values of Staphylococcal nuclease mutants
    • Carra J.H., Privalov P.L. Energetics of denaturation and m values of Staphylococcal nuclease mutants. Biochemistry. 34:1995;2034-2041
    • (1995) Biochemistry , vol.34 , pp. 2034-2041
    • Carra, J.H.1    Privalov, P.L.2
  • 4
    • 0027953952 scopus 로고
    • Three-sate thermodynamic analysis of denaturation of Staphylococcal nuclease mutants
    • Carra J.H., Anderson E.A., Privalov P.L. Three-sate thermodynamic analysis of denaturation of Staphylococcal nuclease mutants. Biochemistry. 33:1994;10842-10850
    • (1994) Biochemistry , vol.33 , pp. 10842-10850
    • Carra, J.H.1    Anderson, E.A.2    Privalov, P.L.3
  • 5
    • 0024315820 scopus 로고
    • Dissection of functional domains of adenovirus DNA polymerase by linker-insertion mutagenesis
    • Chen M., Horwitz M.S. Dissection of functional domains of adenovirus DNA polymerase by linker-insertion mutagenesis. Proc. Natl Acad. Sci. USA. 86:1989;6116-6120
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 6116-6120
    • Chen, M.1    Horwitz, M.S.2
  • 8
    • 0028034697 scopus 로고
    • Reaching out: Locating and lengthening the interdomain linker in AraC protein
    • Eustance R.J., Bustos S.A., Schleif R.F. Reaching out locating and lengthening the interdomain linker in AraC protein. J. Mol. Biol. 242:1994;330-338
    • (1994) J. Mol. Biol. , vol.242 , pp. 330-338
    • Eustance, R.J.1    Bustos, S.A.2    Schleif, R.F.3
  • 10
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C., von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:1989;319-326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 12
    • 0026552361 scopus 로고
    • Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence
    • Heinz D.W., Baase W.A., Matthews W.A. Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. Proc. Natl Acad. Sci. USA. 89:1992;869-886
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 869-886
    • Heinz, D.W.1    Baase, W.A.2    Matthews, W.A.3
  • 13
    • 0027497604 scopus 로고
    • How amino-acid insertions are allowed in an α-helix of T4 lysozyme
    • Heinz D., Baase W.A., Dahlquist F.W., Matthews B.W. How amino-acid insertions are allowed in an α-helix of T4 lysozyme. Nature. 361:1993;561-564
    • (1993) Nature , vol.361 , pp. 561-564
    • Heinz, D.1    Baase, W.A.2    Dahlquist, F.W.3    Matthews, B.W.4
  • 15
    • 0023662556 scopus 로고
    • 1H NMR spectroscopy of conformational changes accompanying substitutions for glutamic acid-43
    • 1H NMR spectroscopy of conformational changes accompanying substitutions for glutamic acid-43. Biochemistry. 26:1987;6278-6286
    • (1987) Biochemistry , vol.26 , pp. 6278-6286
    • Hibler, D.W.1    Stolowich, N.J.2    Reynolds, M.A.3    Gerlt, J.A.4
  • 17
    • 0027467033 scopus 로고
    • The α aneurism: A structural motif revealed in an insertion mutant of Staphylococcal nuclease
    • Keefe L.J., Sondek J., Shortle D., Lattman E. The α aneurism a structural motif revealed in an insertion mutant of Staphylococcal nuclease. Proc. Natl Acad. Sci. USA. 90:1993;3275-3279
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 3275-3279
    • Keefe, L.J.1    Sondek, J.2    Shortle, D.3    Lattman, E.4
  • 18
    • 0028203972 scopus 로고
    • Accommodation of insertion mutations on the surface and in the interior of Staphylococcal nuclease
    • Keefe L.J., Quirk S., Gittis A., Sondek J., Lattman E. Accommodation of insertion mutations on the surface and in the interior of Staphylococcal nuclease. Protein Sci. 3:1994;391-401
    • (1994) Protein Sci. , vol.3 , pp. 391-401
    • Keefe, L.J.1    Quirk, S.2    Gittis, A.3    Sondek, J.4    Lattman, E.5
  • 19
    • 0023875970 scopus 로고
    • Using mini-prep plasmid DNA for sequencing double-stranded templates with sequenase
    • Kraft R., Tardiff J., Krauter K.S., Leinwand L.A. Using mini-prep plasmid DNA for sequencing double-stranded templates with sequenase. Biotechniques. 6:1988;544-546
    • (1988) Biotechniques , vol.6 , pp. 544-546
    • Kraft, R.1    Tardiff, J.2    Krauter, K.S.3    Leinwand, L.A.4
  • 20
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. Molscript a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;916-950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 916-950
    • Kraulis, P.1
  • 21
    • 0025967981 scopus 로고
    • Linker mutagenesis of a bacterial fatty acid transport protein
    • Kumar G., Black P.N. Linker mutagenesis of a bacterial fatty acid transport protein. J. Biol. Chem. 266:1991;1348-1353
    • (1991) J. Biol. Chem. , vol.266 , pp. 1348-1353
    • Kumar, G.1    Black, P.N.2
  • 22
    • 0015041802 scopus 로고
    • Metachromatic agar-diffusion methods for detecting Staphylococcal nuclease activity
    • Lachica R.V.F., Genigeorgis C., Hoeprich P.D. Metachromatic agar-diffusion methods for detecting Staphylococcal nuclease activity. Appl. Microbiol. 21:1971;585-587
    • (1971) Appl. Microbiol. , vol.21 , pp. 585-587
    • Lachica, R.V.F.1    Genigeorgis, C.2    Hoeprich, P.D.3
  • 23
    • 0026793941 scopus 로고
    • Insertional mutagenesis of Bordetella pertussis adenylate cyclase*
    • 224-2250
    • Ladant D., Glaser P., Ullmann A. Insertional mutagenesis of Bordetella pertussis adenylate cyclase* J. Biol. Chem. 267:1992;. 224-2250
    • (1992) J. Biol. Chem. , vol.267
    • Ladant, D.1    Glaser, P.2    Ullmann, A.3
  • 24
    • 0024316597 scopus 로고
    • 2+, and the inhibitor pdTp, refined at 1.65 Å
    • 2+, and the inhibitor pdTp, refined at 1.65 Å Proteins. 5:1989;183-201
    • (1989) Proteins , vol.5 , pp. 183-201
    • Loll, P.J.1    Lattman, E.E.2
  • 25
    • 0025260032 scopus 로고
    • Side chain contributions to the stability of alpha-helical structure in peptides
    • Lyu P.C., Liff M.I., Marky L.A., Kallenbach N.R. Side chain contributions to the stability of alpha-helical structure in peptides. Science. 250:1990;669-673
    • (1990) Science , vol.250 , pp. 669-673
    • Lyu, P.C.1    Liff, M.I.2    Marky, L.A.3    Kallenbach, N.R.4
  • 26
    • 0031588907 scopus 로고    scopus 로고
    • A simple screen for permissive sites in proteins: Analysis of Escherichia coli lac permease
    • Manoil C., Bailey J. A simple screen for permissive sites in proteins Analysis of Escherichia coli lac permease. J. Mol. Biol. 267:1997;250-263
    • (1997) J. Mol. Biol. , vol.267 , pp. 250-263
    • Manoil, C.1    Bailey, J.2
  • 27
    • 0024707204 scopus 로고
    • Unsually stable helix formation in short alanine-based peptides
    • Marqusee S., Robbins V.H., Baldwin R.L. Unsually stable helix formation in short alanine-based peptides. Proc. Natl Acad. Sci. USA. 86:1989;5286-5290
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 5286-5290
    • Marqusee, S.1    Robbins, V.H.2    Baldwin, R.L.3
  • 28
    • 0029967068 scopus 로고    scopus 로고
    • Contributions of the ionizable amino acids to the stability of Staphylococcal nuclease
    • Meeker A.K., Garcia-Moreno E.B., Shortle D. Contributions of the ionizable amino acids to the stability of Staphylococcal nuclease. Biochemistry. 35:1996;6443-6449
    • (1996) Biochemistry , vol.35 , pp. 6443-6449
    • Meeker, A.K.1    Garcia-Moreno, E.B.2    Shortle, D.3
  • 29
    • 0030945611 scopus 로고    scopus 로고
    • Insertion mutagenesis of the lac repressor and its inplications for structure-function analysis
    • Nelson B.D., Manoil C., Traxler B. Insertion mutagenesis of the lac repressor and its inplications for structure-function analysis. J. Bacteriol. 179:1997;3721-3728
    • (1997) J. Bacteriol. , vol.179 , pp. 3721-3728
    • Nelson, B.D.1    Manoil, C.2    Traxler, B.3
  • 30
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occuring amino acids
    • O'Neil K.T., DeGrado W.F. A thermodynamic scale for the helix-forming tendencies of the commonly occuring amino acids. Science. 250:1990;646-651
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    Degrado, W.F.2
  • 32
    • 0026566796 scopus 로고
    • Analysis of insertions/deletions in protein structures
    • Pascarella S., Argos P. Analysis of insertions/deletions in protein structures. J. Mol. Biol. 224:1992;461-471
    • (1992) J. Mol. Biol. , vol.224 , pp. 461-471
    • Pascarella, S.1    Argos, P.2
  • 33
    • 0025357319 scopus 로고
    • Kinetic and conformational effects of lysine substitutions for arginines 35 and 87 in the active site of Staphylococcal nuclease
    • Pourmotabbed T., Dell'Accqua M., Gerlt J.A. Kinetic and conformational effects of lysine substitutions for arginines 35 and 87 in the active site of Staphylococcal nuclease. Biochemistry. 29:1990;3677-3683
    • (1990) Biochemistry , vol.29 , pp. 3677-3683
    • Pourmotabbed, T.1    Dell'Accqua, M.2    Gerlt, J.A.3
  • 34
    • 0024550382 scopus 로고
    • Linker insertion mutagenesis of the human immunodeficiency virus reverse transcriptase expressed in bacteria: Definition of the minimal polymerase domain
    • Prasad V., Goff S.P. Linker insertion mutagenesis of the human immunodeficiency virus reverse transcriptase expressed in bacteria definition of the minimal polymerase domain. Proc. Natl Acad. Sci. USA. 86:1989;3104-3108
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 3104-3108
    • Prasad, V.1    Goff, S.P.2
  • 35
    • 0027173243 scopus 로고
    • AraC protein can activate transcription from only one position and when pointed in only one direction
    • Reeder T.C., Schleif R.F. AraC protein can activate transcription from only one position and when pointed in only one direction. J. Mol. Biol. 231:1993;205-218
    • (1993) J. Mol. Biol. , vol.231 , pp. 205-218
    • Reeder, T.C.1    Schleif, R.F.2
  • 39
    • 0020583027 scopus 로고
    • A genetic system for analysis of Staphylococcal nuclease
    • Shortle D. A genetic system for analysis of Staphylococcal nuclease. Gene. 22:1983;181-189
    • (1983) Gene , vol.22 , pp. 181-189
    • Shortle, D.1
  • 41
    • 0028936999 scopus 로고
    • Staphylococcal nuclease: A showcase of m-value effects
    • Shortle D. Staphylococcal nuclease a showcase of m-value effects. Advan. Protein Chem. 46:1995;217-247
    • (1995) Advan. Protein Chem. , vol.46 , pp. 217-247
    • Shortle, D.1
  • 42
    • 0022994226 scopus 로고
    • Mutants forms of Staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturation
    • Shortle D., Meeker A.K. Mutants forms of Staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturation. Proteins. 1:1986;81-89
    • (1986) Proteins , vol.1 , pp. 81-89
    • Shortle, D.1    Meeker, A.K.2
  • 43
    • 0025005525 scopus 로고
    • Contributions of the large hydrophobic amino acids to the stability of Staphylococcal nuclease
    • Shortle D., Stites W.E., Meeker A.K. Contributions of the large hydrophobic amino acids to the stability of Staphylococcal nuclease. Biochemisrty. 29:1990;8033-8041
    • (1990) Biochemisrty , vol.29 , pp. 8033-8041
    • Shortle, D.1    Stites, W.E.2    Meeker, A.K.3
  • 44
    • 0025339507 scopus 로고
    • Accommodation of single amino acid insertions by the native state of Staphylococcal nuclease
    • Sondek J., Shortle D. Accommodation of single amino acid insertions by the native state of Staphylococcal nuclease. Proteins. 7:1990;299-305
    • (1990) Proteins , vol.7 , pp. 299-305
    • Sondek, J.1    Shortle, D.2
  • 45
    • 0026691077 scopus 로고
    • Structural and energetic differences between insertions and substitutions in Staphylococcal nuclease
    • Sondek J., Shortle D. Structural and energetic differences between insertions and substitutions in Staphylococcal nuclease. Proteins. 13:1992;132-140
    • (1992) Proteins , vol.13 , pp. 132-140
    • Sondek, J.1    Shortle, D.2
  • 46
    • 84934485247 scopus 로고
    • F.A. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, & K. Struhl. New York: John Wiley and Sons
    • Tabor S. Ausubel F.A., Brent R., Kingston R.E., Moore D.D., Seidman J.G., Smith J.A., Struhl K. Current Protocols in Molecular Biology. 1990;John Wiley and Sons, New York
    • (1990) Current Protocols in Molecular Biology
    • Tabor, S.1
  • 47
    • 0024121540 scopus 로고
    • Domain structure of the Moloney murine leukemia virus reverse transcriptase: Mutational analysis and separate expression of the DNA polymerase and RNase H activities
    • Tanese N., Goff S.P. Domain structure of the Moloney murine leukemia virus reverse transcriptase Mutational analysis and separate expression of the DNA polymerase and RNase H activities. Proc. Natl Acad. Sci. USA. 85:1988;1777-1781
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 1777-1781
    • Tanese, N.1    Goff, S.P.2
  • 48
    • 0018275186 scopus 로고
    • Staphylococcal nuclease reviewed: A prototypic study in contemporary enzymology. I. Isolation, physical, and enzymatic properties
    • Tucker P.W., Hazen E.E., Cotton F.A. Staphylococcal nuclease reviewed a prototypic study in contemporary enzymology. I. Isolation, physical, and enzymatic properties. Biochemistry. 22:1978;67-77
    • (1978) Biochemistry , vol.22 , pp. 67-77
    • Tucker, P.W.1    Hazen, E.E.2    Cotton, F.A.3
  • 49
    • 0030462974 scopus 로고    scopus 로고
    • Protein structural plasticity exemplified by insertion and deletion mutants in T4 lysozyme
    • Vetter I.R., Baase W.A., Heinz D.W., Xiong J.P., Snow S., Matthews B.W. Protein structural plasticity exemplified by insertion and deletion mutants in T4 lysozyme. Protein Sci. 5:1996;2399-2415
    • (1996) Protein Sci. , vol.5 , pp. 2399-2415
    • Vetter, I.R.1    Baase, W.A.2    Heinz, D.W.3    Xiong, J.P.4    Snow, S.5    Matthews, B.W.6
  • 50
    • 0025845435 scopus 로고
    • Structure-function studies of human cholesteryl ester transfer protein by linker insertion scanning mutagenesis
    • Wang S., Deng L., Brow M.L., Agellon L.B., Tall A.R. Structure-function studies of human cholesteryl ester transfer protein by linker insertion scanning mutagenesis. Biochemistry. 30:1991;3484-3490
    • (1991) Biochemistry , vol.30 , pp. 3484-3490
    • Wang, S.1    Deng, L.2    Brow, M.L.3    Agellon, L.B.4    Tall, A.R.5
  • 51
    • 0025102790 scopus 로고
    • Diverse interactions between the individual mutations in a double mutant at the active site of Staphylococcal nuclease
    • Weber D.J., Serpersu E.H., Shortle D., Mildvan A.S. Diverse interactions between the individual mutations in a double mutant at the active site of Staphylococcal nuclease. Biochemistry. 29:1990;8632-8642
    • (1990) Biochemistry , vol.29 , pp. 8632-8642
    • Weber, D.J.1    Serpersu, E.H.2    Shortle, D.3    Mildvan, A.S.4
  • 52
    • 0025880704 scopus 로고
    • Interactions of the acid and base catalysts on Staphylococcal nuclease as studied in a double mutant
    • Weber D.J., Meeker A.K., Mildvan A.S. Interactions of the acid and base catalysts on Staphylococcal nuclease as studied in a double mutant. Biochemistry. 30:1991;6103-6114
    • (1991) Biochemistry , vol.30 , pp. 6103-6114
    • Weber, D.J.1    Meeker, A.K.2    Mildvan, A.S.3
  • 53
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC 19 vectors
    • Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains nucleotide sequences of the M13mp18 and pUC 19 vectors. Gene. 33:1985;103-119
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 54
    • 0024368864 scopus 로고
    • Precise gene fusion by PCR
    • Yon J., Fried M. Precise gene fusion by PCR. Nucl. Acids Res. 17:1989;4895
    • (1989) Nucl. Acids Res. , vol.17 , pp. 4895
    • Yon, J.1    Fried, M.2
  • 55
    • 0025730653 scopus 로고
    • Mapping catalytically important regions of an enzyme using two-codon insertion mutagenesis: A case study correlating β-lactamase mutants with the three-dimensional structure
    • Zebela J., Barany F. Mapping catalytically important regions of an enzyme using two-codon insertion mutagenesis a case study correlating β-lactamase mutants with the three-dimensional structure. Gene. 100:1991;51-57
    • (1991) Gene , vol.100 , pp. 51-57
    • Zebela, J.1    Barany, F.2
  • 56
    • 0026018933 scopus 로고
    • Toward a simplication of the protein folding problem: A stabilizing polyalanine α-helix engineered in T4 lysozyme
    • Zhang X-J., Baase W.A., Matthews B.W. Toward a simplication of the protein folding problem a stabilizing polyalanine α-helix engineered in T4 lysozyme. Biochemistry. 30:1991;2012-2017
    • (1991) Biochemistry , vol.30 , pp. 2012-2017
    • Zhang, X.-J.1    Baase, W.A.2    Matthews, B.W.3
  • 57
    • 0027093322 scopus 로고
    • Multiple alanine replacements within a-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability
    • Zhang X-J., Baase W.A., Matthews B.W. Multiple alanine replacements within a-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. Protein Sci. 1:1992;761-776
    • (1992) Protein Sci. , vol.1 , pp. 761-776
    • Zhang, X.-J.1    Baase, W.A.2    Matthews, B.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.