Isolation of a peptide that inhibits the posttranslational arginylation of proteins in rat brain.
All eukaryotic cells contain enzymes that are able to catalyze the transfer of Arg from tRNA to the N-terminus of naturally short lived or damaged cytosolic proteins. For certain test proteins, it has been shown that the addition of Arg to the N-terminus leads to their degradation via the ubiquitin proteolytic pathway. The mechanisms used by cells for identifying proteins for arginylation and regulating arginylation are not known. The present study reports the isolation of a peptide from rat brain that is able to inhibit the arginylation of proteins in brain extracts. We suggest that this peptide is the physiological regulator of arginylation in rat brain.
Yu
M
M
Department of Physiology, New Jersey Medical School-UMDNJ, Newark 07103-2457.
Grabow
M
M
Ingoglia
N A
NA
D000818:Animals; D001120:Arginine / Q000378:metabolism*; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D008297:Male; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000096:biosynthesis* / Q000302:isolation & purification; D010455:Peptides / Q000302:isolation & purification* / Q000494:pharmacology*; D011499:Protein Processing, Post-Translational / Q000187:drug effects* / Q000502:physiology; D012347:RNA, Transfer, Arg / Q000378:metabolism*; D051381:Rats; D017207:Rats, Sprague-Dawley; D014020:Tissue Extracts / Q000494:pharmacology
D009419:Nerve Tissue Proteins; D010455:Peptides; D012347:RNA, Transfer, Arg; D014020:Tissue Extracts; D001120:Arginine