INVESTIGADORES
HALLAK Marta Elena
artículos
Título:
PROTEIN ARGINYLATION IN RAT BRAIN CYTOSOL: A PROTEOMIC ANALYSIS.
Autor/es:
M. B. DECCA, M. GALIANO, C. BOSC, D. JOB, T. RABILLOUD, J. GARIN, AND M. HALLAK
Revista:
NEUROCHEMICAL RESEARCH
Referencias:
Año: 2006 p. 1 - 9
ISSN:
0364-3190
Resumen:
Abstract Arginine can be post-translationally incorporated
from arginyl-tRNA into the N-terminus of soluble acceptor
proteins in a reaction catalyzed by arginyl-tRNA protein
transferase. In the present study, several soluble rat brain
proteins that accepted arginine were identified after arginine
incorporation by two dimensional electrophoresis and mass
spectrometry. They were identified as: contrapsin-like
protease inhibitor-3, a-1-antitrypsin, apolipoprotein E,
hemopexin, calreticulin and apolipoprotein A-I. All of these
proteins shared a signal sequence for the translocation of
proteins across endoplasmic reticulum membranes. After
losing the signal peptide, these proteins expose amino acids
described as compatible for post-translational arginylation.
Although the enzymatic system involved in arginylation is
confined mainly in cytosol and nucleus, all the substrates
described herein enter to the exocytic pathway co-translationally.
Therefore, we postulate that the substrates for
arginylation could reach the cytosol by retro-translocation
and be then arginylated.
Keywords Arginylation Æ Proteomics Æ Brain proteinsArginylation Æ Proteomics Æ Brain proteins
hemopexin, calreticulin and apolipoprotein A-I. All of these
proteins shared a signal sequence for the translocation of
proteins across endoplasmic reticulum membranes. After
losing the signal peptide, these proteins expose amino acids
described as compatible for post-translational arginylation.
Although the enzymatic system involved in arginylation is
confined mainly in cytosol and nucleus, all the substrates
described herein enter to the exocytic pathway co-translationally.
Therefore, we postulate that the substrates for
arginylation could reach the cytosol by retro-translocation
and be then arginylated.
Keywords Arginylation Æ Proteomics Æ Brain proteinsArginylation Æ Proteomics Æ Brain proteins
from arginyl-tRNA into the N-terminus of soluble acceptor
proteins in a reaction catalyzed by arginyl-tRNA protein
transferase. In the present study, several soluble rat brain
proteins that accepted arginine were identified after arginine
incorporation by two dimensional electrophoresis and mass
spectrometry. They were identified as: contrapsin-like
protease inhibitor-3, a-1-antitrypsin, apolipoprotein E,
hemopexin, calreticulin and apolipoprotein A-I. All of these
proteins shared a signal sequence for the translocation of
proteins across endoplasmic reticulum membranes. After
losing the signal peptide, these proteins expose amino acids
described as compatible for post-translational arginylation.
Although the enzymatic system involved in arginylation is
confined mainly in cytosol and nucleus, all the substrates
described herein enter to the exocytic pathway co-translationally.
Therefore, we postulate that the substrates for
arginylation could reach the cytosol by retro-translocation
and be then arginylated.
Keywords Arginylation Æ Proteomics Æ Brain proteinsArginylation Æ Proteomics Æ Brain proteins
hemopexin, calreticulin and apolipoprotein A-I. All of these
proteins shared a signal sequence for the translocation of
proteins across endoplasmic reticulum membranes. After
losing the signal peptide, these proteins expose amino acids
described as compatible for post-translational arginylation.
Although the enzymatic system involved in arginylation is
confined mainly in cytosol and nucleus, all the substrates
described herein enter to the exocytic pathway co-translationally.
Therefore, we postulate that the substrates for
arginylation could reach the cytosol by retro-translocation
and be then arginylated.
Keywords Arginylation Æ Proteomics Æ Brain proteinsArginylation Æ Proteomics Æ Brain proteins
Arginine can be post-translationally incorporated
from arginyl-tRNA into the N-terminus of soluble acceptor
proteins in a reaction catalyzed by arginyl-tRNA protein
transferase. In the present study, several soluble rat brain
proteins that accepted arginine were identified after arginine
incorporation by two dimensional electrophoresis and mass
spectrometry. They were identified as: contrapsin-like
protease inhibitor-3, a-1-antitrypsin, apolipoprotein E,
hemopexin, calreticulin and apolipoprotein A-I. All of these
proteins shared a signal sequence for the translocation of
proteins across endoplasmic reticulum membranes. After
losing the signal peptide, these proteins expose amino acids
described as compatible for post-translational arginylation.
Although the enzymatic system involved in arginylation is
confined mainly in cytosol and nucleus, all the substrates
described herein enter to the exocytic pathway co-translationally.
Therefore, we postulate that the substrates for
arginylation could reach the cytosol by retro-translocation
and be then arginylated.
Keywords Arginylation Æ Proteomics Æ Brain proteinsArginylation Æ Proteomics Æ Brain proteins
hemopexin, calreticulin and apolipoprotein A-I. All of these
proteins shared a signal sequence for the translocation of
proteins across endoplasmic reticulum membranes. After
losing the signal peptide, these proteins expose amino acids
described as compatible for post-translational arginylation.
Although the enzymatic system involved in arginylation is
confined mainly in cytosol and nucleus, all the substrates
described herein enter to the exocytic pathway co-translationally.
Therefore, we postulate that the substrates for
arginylation could reach the cytosol by retro-translocation
and be then arginylated.
Keywords Arginylation Æ Proteomics Æ Brain proteinsArginylation Æ Proteomics Æ Brain proteins
a-1-antitrypsin, apolipoprotein E,
hemopexin, calreticulin and apolipoprotein A-I. All of these
proteins shared a signal sequence for the translocation of
proteins across endoplasmic reticulum membranes. After
losing the signal peptide, these proteins expose amino acids
described as compatible for post-translational arginylation.
Although the enzymatic system involved in arginylation is
confined mainly in cytosol and nucleus, all the substrates
described herein enter to the exocytic pathway co-translationally.
Therefore, we postulate that the substrates for
arginylation could reach the cytosol by retro-translocation
and be then arginylated.
Keywords Arginylation Æ Proteomics Æ Brain proteinsArginylation Æ Proteomics Æ Brain proteins