Preliminary 2D Structure Analysis Of Several Transcription Elongation Factors

Eukaryotic transcription elongation process is regulated by a variety of protein complexes.RNA polymerase ?,the central factor of transcription,interferes with different protein complexes(Set2,Ctk1 kinase complex,Burl kinase complex,and basic transcription elongation factor Spt5/4)in both direct and indirect way.We focus on the study of RNAPII CTD phosphorylation,catalyzed by Ctkl kinase complex,including their structure states and the regulatory mechanism of transcription.Spt5 contains a CTD domain that can be phosphorylated just as RNAPII,such modification plays an important role in the assembly of the transcription machinery and transcription regulation.I purified general transcription elongation factor Spt5/4 and its kinase Burl complex in vivo and tested its biological activity.Then I analyzed its approximate 2D average.It lays a foundation for further research of the structure and function.Set2 is methyltransferase of H3K36.In vivo,it exists in two conformations:free or Set2-RNAPII complex.Previous research of its function has suggested that different conformations play different roles.But it's still unknown that the regulation mechanism of Set2 and Set2-RNAPII and their structure.I purified Set2 and Set2-RNAPII complex from yeast,and analyzed their 2D structure.It provides the possibility for further research of the regulation mechanism between RNAPII and Set2.