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Title: Sequence of a benzyladenine binding site peptide isolated from a wheat embyro cytokinin-binding protein

Abstract

A wheat embryo cytokinin-binding protein (CBF-1) was covalently modified with the radiolabeled photoaffinity ligand (/sup 14/C)-2-azido-N/sup 6/-benzyladenine (AzBA). A single labeled peptide was obtained after proteolytic digestion and isolation by reversed-phase and anion exchange HPLC. Sequencing by Edman degradation identified 11 of the 12 residues, but failed to identify the labeled amino acid. Amino acid analysis and sequencing by laser photodissociation-Fourier transform mass spectrometry conclusively identified the labeled residue as the histidine: Ala-Phe-Leu-Gln-Pro-Ser-His-His*-Asp-Ala-Asp-Glu. Comparison of this sequence with the known partial primary sequence of CBF-1 (determined by tandem quadrupole mass spectrometry) showed that there were two homologous sequences in CBF-1. One exactly matched the above AzBA labeled peptide and the other differed by a substitution of tyrosine for the second histidine. The possibility of binding and non-binding CBF-1 isomers will be discussed along with a proposed model for BA binding.

Authors:
; ; ; ; ;
Publication Date:
Research Org.:
Cell Research Institute, Dublin, CA
OSTI Identifier:
5653449
Report Number(s):
CONF-8707108-
Journal ID: CODEN: PPYSA
Resource Type:
Conference
Journal Name:
Plant Physiol., Suppl.; (United States)
Additional Journal Information:
Journal Volume: 83:4; Conference: Annual meeting of the American Society of Plant Physiologists, St. Louis, MO, USA, 19 Jul 1987
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; PLANT GROWTH REGULATORS; BIOCHEMICAL REACTION KINETICS; PROTEINS; AMINO ACID SEQUENCE; AMINO ACIDS; CARBON 14 COMPOUNDS; DIGESTION; KININS; LASER RADIATION; LIGANDS; LIQUID COLUMN CHROMATOGRAPHY; MASS SPECTROSCOPY; PEPTIDES; TRACER TECHNIQUES; WHEAT; CARBOXYLIC ACIDS; CEREALS; CHROMATOGRAPHY; ELECTROMAGNETIC RADIATION; GRASS; ISOTOPE APPLICATIONS; KINETICS; LABELLED COMPOUNDS; MOLECULAR STRUCTURE; ORGANIC ACIDS; ORGANIC COMPOUNDS; PLANTS; POLYPEPTIDES; RADIATIONS; REACTION KINETICS; SEPARATION PROCESSES; SPECTROSCOPY; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Brinegar, A C, Fox, J E, Cooper, G, Hunt, D F, Shabanowitz, J, and Hauer, C M. Sequence of a benzyladenine binding site peptide isolated from a wheat embyro cytokinin-binding protein. United States: N. p., 1987. Web.
Brinegar, A C, Fox, J E, Cooper, G, Hunt, D F, Shabanowitz, J, & Hauer, C M. Sequence of a benzyladenine binding site peptide isolated from a wheat embyro cytokinin-binding protein. United States.
Brinegar, A C, Fox, J E, Cooper, G, Hunt, D F, Shabanowitz, J, and Hauer, C M. Wed . "Sequence of a benzyladenine binding site peptide isolated from a wheat embyro cytokinin-binding protein". United States.
@article{osti_5653449,
title = {Sequence of a benzyladenine binding site peptide isolated from a wheat embyro cytokinin-binding protein},
author = {Brinegar, A C and Fox, J E and Cooper, G and Hunt, D F and Shabanowitz, J and Hauer, C M},
abstractNote = {A wheat embryo cytokinin-binding protein (CBF-1) was covalently modified with the radiolabeled photoaffinity ligand (/sup 14/C)-2-azido-N/sup 6/-benzyladenine (AzBA). A single labeled peptide was obtained after proteolytic digestion and isolation by reversed-phase and anion exchange HPLC. Sequencing by Edman degradation identified 11 of the 12 residues, but failed to identify the labeled amino acid. Amino acid analysis and sequencing by laser photodissociation-Fourier transform mass spectrometry conclusively identified the labeled residue as the histidine: Ala-Phe-Leu-Gln-Pro-Ser-His-His*-Asp-Ala-Asp-Glu. Comparison of this sequence with the known partial primary sequence of CBF-1 (determined by tandem quadrupole mass spectrometry) showed that there were two homologous sequences in CBF-1. One exactly matched the above AzBA labeled peptide and the other differed by a substitution of tyrosine for the second histidine. The possibility of binding and non-binding CBF-1 isomers will be discussed along with a proposed model for BA binding.},
doi = {},
journal = {Plant Physiol., Suppl.; (United States)},
number = ,
volume = 83:4,
place = {United States},
year = {1987},
month = {4}
}

Conference:
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