High impact information on Su(Tpl)

• Interestingly, we find that dELL co-localizes extensively with the phosphorylated, actively elongating form of Pol II at transcriptionally active sites on Drosophila polytene chromosomes [1].
• Drosophila ELL is associated with actively elongating RNA polymerase II on transcriptionally active sites in vivo [1].
• This observation indicates a dynamic pattern of localization of dELL in cells, which is a predicted characteristic of a Pol II general elongation factor [1].
• dELL is an essential RNA polymerase II elongation factor with a general role in development [2].
• The purpose of this study was to test whether an ELL family protein is required for gene expression in vivo [2].

Biological context of Su(Tpl)

• Binding of the RNA Polymerase II elongation factor ELL was reduced in knockdown chromosomes, suggesting that ELL is recruited to active polymerase via CTD phosphorylation [3].
• We have characterized seven distinct mutant alleles of Su(Tpl) and show that a dELL transgene rescues recessive lethality of Su(Tpl) [2].
• Deletion studies have defined domains in mammalian ELL required for transcription elongation activity and RNA polymerase binding in vitro, for transformation of cultured cells when overexpressed, and for leukemogenesis and cell proliferation as part of a leukemic fusion protein [4].
• We demonstrate that a central domain of dELL is required for rapid mobilization of ELL during the heat shock response, suggesting a regulatory function for this domain [4].
• These P-element deletions can now be used to isolate dELL mutations by EMS mutagenesis [5].

Analytical, diagnostic and therapeutic context of Su(Tpl)

• We showed that dELL is expressed mainly in the ovaries and early embryonic stages by developmental Northern blot. dELL encodes a protein of 912 amino acids which is substantially longer than the hELL (612 aa) [5].

References