Proteomics Studies of the Interactome of RNA Polymerase II C-Terminal Repeated Domain

ABSTRACT: We developed a proteomics approach to examine the mammalian CTD-interactome. We used six synthetic peptides each consisting of four consensus CTD-repeats and with different combinations of serine and tyrosine phosphorylation as affinity-matrix to pull-down nuclear proteins from HeLa cells. The pull-down fractions were then analyzed by MUDPIT mass spectrometry. This approach identified a total of 100 CTD-interacting proteins pull-downed by the differentially phosphorylated CTD-peptides. Our analyses showed that the majority of proteins pulled-down by serine-phosphorylatd CTD are involved in RNA processing. Furthermore, this study identified proteins that were preferentially pulled-down by tyrosine/serine-doubly phosphorylated CTD.

INSTRUMENT(S): LTQ

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Jean Y. J. Wang 

PROVIDER: MSV000078867 | MassIVE |

REPOSITORIES: MassIVE