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Glyceraldehyde‐3‐phosphate dehydrogenase and actin associate with RNA polymerase II and interact with its Rpb7 subunit
Author(s) -
Mitsuzawa Hiroshi,
Kimura Makoto,
Kanda Emi,
Ishihama Akira
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.11.045
Subject(s) - glyceraldehyde 3 phosphate dehydrogenase , rna polymerase ii , transcription factor ii f , microbiology and biotechnology , biology , transcription factor ii d , biochemistry , protein subunit , rna polymerase ii holoenzyme , polymerase , dehydrogenase , rna dependent rna polymerase , enzyme , promoter , gene expression , gene
RNA polymerase II (pol II) purified from the fission yeast Schizosaccharomyces pombe was previously reported to be associated with the general transcription factor TFIIF and the C‐terminal domain phosphatase Fcp1, as well as glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH), which has recently been implicated in transcriptional activation in human cells. Here, we provide evidence that the Rpb7 subunit of pol II interacts with GAPDH. Two‐hybrid screen identified GAPDH as an Rpb7‐binding protein. In addition, GAPDH was affinity‐purified from S. pombe extract by using an Rpb4/Rpb7‐coupled column. We also identified actin as a pol II‐associated protein and revealed the interaction between actin and Rpb7.