Literature DB >> 489535

7-Methylguanosine-dependent inhibition of globin mRNA translation by methylglyoxal.

J W Kozarich, J L Deegan.   

Abstract

Studies on the inhibition of translation by methylglyoxal of capped and chemically decapped globin mRNAs in the rabbit reciculocyte system strongly suggest that it is cap-dependent. Concentrations of methylglyoxal (0.2 mM), which effected substantial inhibition (80%) of capped mRNA, were only slightly inhibitory (10%) to the decapped species. In addition, the inhibition was K+-dependent with maximal inhibition occurring at the K+ optimum for translation of the capped species, suggesting cap recognition is required for the effect. Results with endogenous mRNA further substantiate that initiation and not elongation is the site of action. These results are consistent with an inhibition due to a newly discovered, rapid reaction of methylglyoxal with the 7-methylguanosine of the cap structure.

Entities:  

Mesh:

Substances:

Year:  1979        PMID: 489535

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  3 in total

Review 1.  The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life.

Authors:  P J Thornalley
Journal:  Biochem J       Date:  1990-07-01       Impact factor: 3.857

2.  A comparative study on proliferation, macromolecular synthesis and energy metabolism of in vitro-grown Ehrlich ascites tumor cells in the presence of glucosone, galactosone and methylglyoxal.

Authors:  K A Reiffen; F Schneider
Journal:  J Cancer Res Clin Oncol       Date:  1984       Impact factor: 4.553

3.  Probing the active site of glyoxalase I from human erythrocytes by use of the strong reversible inhibitor S-p-bromobenzylglutathione and metal substitutions.

Authors:  A C Aronsson; S Sellin; G Tibbelin; B Mannervik
Journal:  Biochem J       Date:  1981-07-01       Impact factor: 3.857

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.