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Charlotte Rohde Knudsen

Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Standard

Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA. / Wiborg, Ove; Andersen, C; Knudsen, Charlotte Rohde; Clark, Brian F. C.; Nyborg, Jens.

I: Journal of Biological Chemistry, Bind 271, Nr. 34, 1996, s. 20406-11.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Wiborg, O, Andersen, C, Knudsen, CR, Clark, BFC & Nyborg, J 1996, 'Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA.', Journal of Biological Chemistry, bind 271, nr. 34, s. 20406-11.

APA

Wiborg, O., Andersen, C., Knudsen, C. R., Clark, B. F. C., & Nyborg, J. (1996). Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA. Journal of Biological Chemistry, 271(34), 20406-11.

CBE

Wiborg O, Andersen C, Knudsen CR, Clark BFC, Nyborg J. 1996. Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA. Journal of Biological Chemistry. 271(34):20406-11.

MLA

Wiborg, Ove o.a.. "Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA.". Journal of Biological Chemistry. 1996, 271(34). 20406-11.

Vancouver

Wiborg O, Andersen C, Knudsen CR, Clark BFC, Nyborg J. Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA. Journal of Biological Chemistry. 1996;271(34):20406-11.

Author

Wiborg, Ove ; Andersen, C ; Knudsen, Charlotte Rohde ; Clark, Brian F. C. ; Nyborg, Jens. / Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA. I: Journal of Biological Chemistry. 1996 ; Bind 271, Nr. 34. s. 20406-11.

Bibtex

@article{3638d660da4711dcbc43000ea68e967b,
title = "Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA.",
abstract = "Two residues of Escherichia coli elongation factor Tu involved in binding of aminoacyl-tRNA were identified and subjected to mutational analysis. Lys-89 and Asn-90 were each replaced by either Ala or Glu. The four single mutants were denoted K89A, K89E, N90A, and N90E, respectively. The mutants were characterized with respect to thermal and chemical stability, GTPase activity, tRNA affinity, and activity in an in vitro translation assay. Most conspicuously tRNA affinities were reduced for all mutants. The results verify our structural analysis of elongation factor Tu in complex with aminoacyl-tRNA, which suggested an important role of Lys-89 and Asn-90 in tRNA binding. Furthermore, our results indicate helix B to be an important target site for nucleotide exchange factor EF-Ts. Also the mutants His-66 to Ala and His-118 to either Ala or Glu were characterized in an in vitro translation assay. Their functional roles are discussed in relation to the structure of elongation factor Tu in complex with aminoacyl-tRNA. Udgivelsesdato: 1996-Aug-23",
keywords = "Amino Acid Sequence, Binding Sites, Escherichia coli, GTP Phosphohydrolase-Linked Elongation Factors, Kinetics, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Peptide Chain Elongation, Translational, Peptide Elongation Factor Tu, Protein Binding, RNA, Transfer, Amino Acyl, Structure-Activity Relationship",
author = "Ove Wiborg and C Andersen and Knudsen, {Charlotte Rohde} and Clark, {Brian F. C.} and Jens Nyborg",
year = "1996",
language = "English",
volume = "271",
pages = "20406--11",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "34",

}

RIS

TY - JOUR

T1 - Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA.

AU - Wiborg, Ove

AU - Andersen, C

AU - Knudsen, Charlotte Rohde

AU - Clark, Brian F. C.

AU - Nyborg, Jens

PY - 1996

Y1 - 1996

N2 - Two residues of Escherichia coli elongation factor Tu involved in binding of aminoacyl-tRNA were identified and subjected to mutational analysis. Lys-89 and Asn-90 were each replaced by either Ala or Glu. The four single mutants were denoted K89A, K89E, N90A, and N90E, respectively. The mutants were characterized with respect to thermal and chemical stability, GTPase activity, tRNA affinity, and activity in an in vitro translation assay. Most conspicuously tRNA affinities were reduced for all mutants. The results verify our structural analysis of elongation factor Tu in complex with aminoacyl-tRNA, which suggested an important role of Lys-89 and Asn-90 in tRNA binding. Furthermore, our results indicate helix B to be an important target site for nucleotide exchange factor EF-Ts. Also the mutants His-66 to Ala and His-118 to either Ala or Glu were characterized in an in vitro translation assay. Their functional roles are discussed in relation to the structure of elongation factor Tu in complex with aminoacyl-tRNA. Udgivelsesdato: 1996-Aug-23

AB - Two residues of Escherichia coli elongation factor Tu involved in binding of aminoacyl-tRNA were identified and subjected to mutational analysis. Lys-89 and Asn-90 were each replaced by either Ala or Glu. The four single mutants were denoted K89A, K89E, N90A, and N90E, respectively. The mutants were characterized with respect to thermal and chemical stability, GTPase activity, tRNA affinity, and activity in an in vitro translation assay. Most conspicuously tRNA affinities were reduced for all mutants. The results verify our structural analysis of elongation factor Tu in complex with aminoacyl-tRNA, which suggested an important role of Lys-89 and Asn-90 in tRNA binding. Furthermore, our results indicate helix B to be an important target site for nucleotide exchange factor EF-Ts. Also the mutants His-66 to Ala and His-118 to either Ala or Glu were characterized in an in vitro translation assay. Their functional roles are discussed in relation to the structure of elongation factor Tu in complex with aminoacyl-tRNA. Udgivelsesdato: 1996-Aug-23

KW - Amino Acid Sequence

KW - Binding Sites

KW - Escherichia coli

KW - GTP Phosphohydrolase-Linked Elongation Factors

KW - Kinetics

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Mutagenesis, Site-Directed

KW - Peptide Chain Elongation, Translational

KW - Peptide Elongation Factor Tu

KW - Protein Binding

KW - RNA, Transfer, Amino Acyl

KW - Structure-Activity Relationship

M3 - Journal article

VL - 271

SP - 20406

EP - 20411

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 34

ER -