Covalent attachment of fluorescent probes to the X-base of escherichia coli phenylalanine transfer ribonucleic acid

Peter W. Schiller; Alan N. Schechter

doi:10.1093/nar/4.7.2161

Covalent attachment of fluorescent probes to the X-base of escherichia coli phenylalanine transfer ribonucleic acid

Peter W. Schiller
, Alan N. Schechter

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

Abstract

tRNAE. coliPhe was labeled with the N-hydroxysuccinimide esters of 1-dimethylaminaphthalene-5-sulfonyl glycine and N-methylanthranilic acid through reaction with the amino acid moiety of its X-base, whereby yields of 66% and 24%, respectively, were obtained. The purified dimethylaminonaphthalene-sulfonate derivative could not be aminoacylated and was found to a strong competitive inhibitor of phenyialanine-tRNA synthetase [K_i=8×10^-7 M]. The N-methylanthraniloyl could be charged to an exten of 5% as compared to native tRNA^Phe. The fluorescence emission spectra of the derivatives are indicative of a slightly hydrophobic environment for both fluorophores. The results suggest that the integrity of the polar amino acid group of the X-base is required for the maintenance of the biologically active conformation.

Original language	English
Pages (from-to)	2161-2168
Number of pages	8
Journal	Nucleic Acids Research
Volume	4
Issue number	7
DOIs	https://doi.org/10.1093/nar/4.7.2161
State	Published - Jul 1977
Externally published	Yes

Access to Document

10.1093/nar/4.7.2161

Cite this

@article{edfadd26e2a24fb59139e72a1e07075d,

title = "Covalent attachment of fluorescent probes to the X-base of escherichia coli phenylalanine transfer ribonucleic acid",

abstract = "tRNAE. coliPhe was labeled with the N-hydroxysuccinimide esters of 1-dimethylaminaphthalene-5-sulfonyl glycine and N-methylanthranilic acid through reaction with the amino acid moiety of its X-base, whereby yields of 66\% and 24\%, respectively, were obtained. The purified dimethylaminonaphthalene-sulfonate derivative could not be aminoacylated and was found to a strong competitive inhibitor of phenyialanine-tRNA synthetase [Ki=8×10-7 M]. The N-methylanthraniloyl could be charged to an exten of 5\% as compared to native tRNAPhe. The fluorescence emission spectra of the derivatives are indicative of a slightly hydrophobic environment for both fluorophores. The results suggest that the integrity of the polar amino acid group of the X-base is required for the maintenance of the biologically active conformation.",

author = "Schiller, \{Peter W.\} and Schechter, \{Alan N.\}",

year = "1977",

month = jul,

doi = "10.1093/nar/4.7.2161",

language = "English",

volume = "4",

pages = "2161--2168",

journal = "Nucleic Acids Research",

issn = "0305-1048",

publisher = "Oxford University Press",

number = "7",

}

TY - JOUR

T1 - Covalent attachment of fluorescent probes to the X-base of escherichia coli phenylalanine transfer ribonucleic acid

AU - Schiller, Peter W.

AU - Schechter, Alan N.

PY - 1977/7

Y1 - 1977/7

N2 - tRNAE. coliPhe was labeled with the N-hydroxysuccinimide esters of 1-dimethylaminaphthalene-5-sulfonyl glycine and N-methylanthranilic acid through reaction with the amino acid moiety of its X-base, whereby yields of 66% and 24%, respectively, were obtained. The purified dimethylaminonaphthalene-sulfonate derivative could not be aminoacylated and was found to a strong competitive inhibitor of phenyialanine-tRNA synthetase [Ki=8×10-7 M]. The N-methylanthraniloyl could be charged to an exten of 5% as compared to native tRNAPhe. The fluorescence emission spectra of the derivatives are indicative of a slightly hydrophobic environment for both fluorophores. The results suggest that the integrity of the polar amino acid group of the X-base is required for the maintenance of the biologically active conformation.

AB - tRNAE. coliPhe was labeled with the N-hydroxysuccinimide esters of 1-dimethylaminaphthalene-5-sulfonyl glycine and N-methylanthranilic acid through reaction with the amino acid moiety of its X-base, whereby yields of 66% and 24%, respectively, were obtained. The purified dimethylaminonaphthalene-sulfonate derivative could not be aminoacylated and was found to a strong competitive inhibitor of phenyialanine-tRNA synthetase [Ki=8×10-7 M]. The N-methylanthraniloyl could be charged to an exten of 5% as compared to native tRNAPhe. The fluorescence emission spectra of the derivatives are indicative of a slightly hydrophobic environment for both fluorophores. The results suggest that the integrity of the polar amino acid group of the X-base is required for the maintenance of the biologically active conformation.

UR - https://www.scopus.com/pages/publications/0017412815

U2 - 10.1093/nar/4.7.2161

DO - 10.1093/nar/4.7.2161

M3 - Article

C2 - 333386

AN - SCOPUS:0017412815

SN - 0305-1048

VL - 4

SP - 2161

EP - 2168

JO - Nucleic Acids Research

JF - Nucleic Acids Research

IS - 7

ER -

Covalent attachment of fluorescent probes to the X-base of escherichia coli phenylalanine transfer ribonucleic acid

Abstract

Access to Document

Fingerprint

Cite this