Physical and functional interaction between elongator and the chromatin-associated Kti12 protein Journal Article
| Authors: | Petrakis, T. G.; Søgaard, T. M. M.; Erdjument-Bromage, H.; Tempst, P.; Svejstrup, J. Q. |
| Article Title: | Physical and functional interaction between elongator and the chromatin-associated Kti12 protein |
| Abstract: | Cells lacking KTI12 or Elongator (ELP) genes are insensitive to the toxin zymocin and also share more general phenotypes. Moreover, data from low stringency immunoprecipitation experiments suggest that Elongator and Kti12 may interact. However, the precise relationship between these factors has not been determined. Here we use a variety of approaches to investigate the possibility that Elongator and Kti12 functionally overlap. Native Kti12 purified to virtual homogeneity under stringent conditions is a single polypeptide, but depletion of Kti12 from a yeast extract results in co-depletion of Elongator, indicating that these factors do interact. Indeed, biochemical evidence suggests that Elongator and Kti12 form a fragile complex under physiological salt conditions. Purified Kti12 does not affect Elongator histone acetyltransferase activity in vitro. However, a variety of genetic experiments comparing the effects of mutation in ELP3 and KTI12 alone and in combination with other transcription factor mutations clearly demonstrate a significant functional overlap between Elongator and Kti12 in vivo. Intriguingly, chromatin immunoprecipitation experiments show that Kti12 is associated with chromatin throughout the genome, even in non-transcribed regions and in the absence of Elongator. Conversely, RNA-immunoprecipitation experiments indicate that Kti12 only plays a minor role for Elongator association with active genes. Together, these experiments indicate a close physical and functional relationship between Elongator and the highly conserved Eti12 protein. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc. |
| Keywords: | unclassified drug; genetics; mutation; nonhuman; proteins; phenotype; metabolism; gene; genes; protein protein interaction; protein binding; genotype; gene product; cytotoxicity; enzyme activity; physiology; rna; immunology; chemistry; saccharomyces cerevisiae; histone; chromatin; gene interaction; western blotting; immunoprecipitation; multiprotein complexes; saccharomyces cerevisiae proteins; saccharomyces cerevisiae protein; point mutation; matrix assisted laser desorption ionization time of flight mass spectrometry; genetic screening; rna polymerase ii; mutagenesis; acyltransferase; acetyltransferases; kluyveromyces; polyacrylamide gel electrophoresis; fungal gene; elongation factor; cells; multiprotein complex; genes, fungal; toxin; histone acetyltransferase; histone acetyltransferases; zymocin; precipitation (chemical); elongators; genetic experiments; kti12 protein; kti12 protein, s cerevisiae; elp gene; kti12 gene; peptide elongation factors |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 280 |
| Issue: | 20 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 2005-05-20 |
| Start Page: | 19454 |
| End Page: | 19460 |
| Language: | English |
| DOI: | 10.1074/jbc.M413373200 |
| PUBMED: | 15772087 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | --- - "Cited By (since 1996): 12" - "Export Date: 24 October 2012" - "CODEN: JBCHA" - "Source: Scopus" |
