Literature DB >> 8292492

Isolation of a peptide that inhibits the posttranslational arginylation of proteins in rat brain.

M Yu1, M Grabow, N A Ingoglia.   

Abstract

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.

Entities:  

Mesh:

Substances:

Year:  1993        PMID: 8292492     DOI: 10.1007/BF02782502

Source DB:  PubMed          Journal:  J Mol Neurosci        ISSN: 0895-8696            Impact factor:   3.444


  19 in total

Review 1.  The ubiquitin system for protein degradation.

Authors:  A Hershko; A Ciechanover
Journal:  Annu Rev Biochem       Date:  1992       Impact factor: 23.643

2.  Ubiquitin is associated with aggregates of arginine modified proteins in injured nerves.

Authors:  D L Jack; G Chakraborty; N A Ingoglia
Journal:  Neuroreport       Date:  1992-01       Impact factor: 1.837

3.  Evidence that axonal tRNAs are resistant to RNase and ATPase and can be aminoacylated in the absence of exogenous ATP.

Authors:  G Chakraborty; A Nicola; N A Ingoglia
Journal:  J Neurochem       Date:  1992-07       Impact factor: 5.372

4.  Protein modification by amino acid addition is increased in crushed sciatic but not optic nerves.

Authors:  S Shyne-Athwal; R V Riccio; G Chakraborty; N A Ingoglia
Journal:  Science       Date:  1986-02-07       Impact factor: 47.728

5.  Amino acid modification of proteins in regenerating sciatic nerves of rats.

Authors:  G Chakraborty; M Yu; D Luo; J A Sturman; N A Ingoglia
Journal:  J Neurosci Res       Date:  1990-04       Impact factor: 4.164

6.  Comparison of posttranslational protein modification by amino acid addition after crush injury to sciatic and optic nerves of rats.

Authors:  S Shyne-Athwal; G Chakraborty; E Gage; N A Ingoglia
Journal:  Exp Neurol       Date:  1988-02       Impact factor: 5.330

7.  A simplified method for the quantitative assay of small amounts of protein in biologic material.

Authors:  G R Schacterle; R L Pollack
Journal:  Anal Biochem       Date:  1973-02       Impact factor: 3.365

8.  Incorporation of 3H-amino acids into proteins in a partially purified fraction of axoplasm: evidence for transfer RNA-mediated, post-translational protein modification in squid giant axons.

Authors:  N A Ingoglia; A Giuditta; M F Zanakis; A Babigian; I Tasaki; G Chakraborty; J A Sturman
Journal:  J Neurosci       Date:  1983-12       Impact factor: 6.167

Review 9.  N-terminal arginylation and ubiquitin-mediated proteolysis in nerve regeneration.

Authors:  G Chakraborty; N A Ingoglia
Journal:  Brain Res Bull       Date:  1993       Impact factor: 4.077

10.  Ubiquitin as a degradation signal.

Authors:  E S Johnson; B Bartel; W Seufert; A Varshavsky
Journal:  EMBO J       Date:  1992-02       Impact factor: 11.598

View more
  1 in total

Review 1.  Posttranslational arginylation as a global biological regulator.

Authors:  Sougata Saha; Anna Kashina
Journal:  Dev Biol       Date:  2011-07-18       Impact factor: 3.582

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.