Structural analysis of the messenger RNA cap-binding protein: presence of phosphate, sulfhydryl, and disulfide groups
Abstract
The messenger-RNA cap-binding protein (CBP) was isolated from human erythrocyte, rabbit erythrocyte, and rabbit reticulocyte lysate by affinity chromatography on 7-methylguanosine 5'-triphosphate-Sepharose. The specific activity of binding to capped oligonucleotides was similar for the human erythrocyte and rabbit reticulocyte CBPs. Isoelectric focusing of human and rabbit preparations revealed that each was composed of up to five species. The pI values of human and rabbit CBPs ranged from 5.7 to 6.5. The predominant form in erythrocytes had a pI of 6.3 while in reticulocytes, two major species, having pI values of 5.9 and 6.3, were present. Labeling of rabbit reticulocytes with (/sup 32/P)orthophosphate revealed that the pI 5.9 but not the pI 6.3 form contained phosphate. All of the phosphate was found in phosphoserine residues. The amino acid compositions of human erythrocyte and rabbit reticulocyte CBPs were quite similar. Both proteins had 7 tryptophanyl and 6 cysteinyl residues. Labeling with (1-/sup 14/C)iodoacetic acid under native and denaturing conditions provided evidence that 2 of the cysteinyl residues are present in the reduced form and 4 in disulfide bridges.
- Publication Date:
- Research Org.:
- Univ. of Kentucky, Lexington
- OSTI Identifier:
- 5150816
- Resource Type:
- Conference
- Journal Name:
- J. Biol. Chem.; (United States)
- Additional Journal Information:
- Journal Volume: 261:1
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; MESSENGER-RNA; BIOCHEMICAL REACTION KINETICS; PROTEINS; STRUCTURAL CHEMICAL ANALYSIS; AMINO ACIDS; CARBON 14 COMPOUNDS; CHROMATOGRAPHY; CYSTEINE; ERYTHROCYTES; EXPERIMENTAL DATA; LABELLED COMPOUNDS; PHOSPHORUS 32; PROTEIN STRUCTURE; RABBITS; RETICULOCYTES; TRACER TECHNIQUES; TRYPTOPHAN; ANIMALS; AROMATICS; AZAARENES; AZOLES; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; BIOLOGICAL MATERIALS; BLOOD; BLOOD CELLS; BODY FLUIDS; CARBOXYLIC ACIDS; DATA; DAYS LIVING RADIOISOTOPES; HETEROCYCLIC ACIDS; HETEROCYCLIC COMPOUNDS; INDOLES; INFORMATION; ISOTOPE APPLICATIONS; ISOTOPES; KINETICS; LIGHT NUCLEI; MAMMALS; MATERIALS; NUCLEI; NUCLEIC ACIDS; NUMERICAL DATA; ODD-ODD NUCLEI; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; ORGANIC SULFUR COMPOUNDS; PHOSPHORUS ISOTOPES; PYRROLES; RADIOISOTOPES; REACTION KINETICS; RNA; SEPARATION PROCESSES; THIOLS; VERTEBRATES; 550201* - Biochemistry- Tracer Techniques
Citation Formats
. Structural analysis of the messenger RNA cap-binding protein: presence of phosphate, sulfhydryl, and disulfide groups. United States: N. p., 1986.
Web.
. Structural analysis of the messenger RNA cap-binding protein: presence of phosphate, sulfhydryl, and disulfide groups. United States.
. 1986.
"Structural analysis of the messenger RNA cap-binding protein: presence of phosphate, sulfhydryl, and disulfide groups". United States.
@article{osti_5150816,
title = {Structural analysis of the messenger RNA cap-binding protein: presence of phosphate, sulfhydryl, and disulfide groups},
author = {},
abstractNote = {The messenger-RNA cap-binding protein (CBP) was isolated from human erythrocyte, rabbit erythrocyte, and rabbit reticulocyte lysate by affinity chromatography on 7-methylguanosine 5'-triphosphate-Sepharose. The specific activity of binding to capped oligonucleotides was similar for the human erythrocyte and rabbit reticulocyte CBPs. Isoelectric focusing of human and rabbit preparations revealed that each was composed of up to five species. The pI values of human and rabbit CBPs ranged from 5.7 to 6.5. The predominant form in erythrocytes had a pI of 6.3 while in reticulocytes, two major species, having pI values of 5.9 and 6.3, were present. Labeling of rabbit reticulocytes with (/sup 32/P)orthophosphate revealed that the pI 5.9 but not the pI 6.3 form contained phosphate. All of the phosphate was found in phosphoserine residues. The amino acid compositions of human erythrocyte and rabbit reticulocyte CBPs were quite similar. Both proteins had 7 tryptophanyl and 6 cysteinyl residues. Labeling with (1-/sup 14/C)iodoacetic acid under native and denaturing conditions provided evidence that 2 of the cysteinyl residues are present in the reduced form and 4 in disulfide bridges.},
doi = {},
url = {https://www.osti.gov/biblio/5150816},
journal = {J. Biol. Chem.; (United States)},
number = ,
volume = 261:1,
place = {United States},
year = {Sun Jan 05 00:00:00 EST 1986},
month = {Sun Jan 05 00:00:00 EST 1986}
}