Questions, Feedback & Help
Send us an email and we'll get back to you ASAP. Or you can read our Frequently Asked Questions.
  • page settings
  • hide sidebar
  • show empty fields
  • layout
  • (too narrow)
  • open all
  • close all
Resources » Paper

Ramadin, V. et al. (2019) International Worm Meeting "The search for additional proteins that physically associate with the LIM-7 transcriptional complex."

  • History

  • Referenced

  • Tree Display

  • My Favorites

  • My Library

  • Comments on Ramadin, V. et al. (2019) International Worm Meeting "The search for additional proteins that physically associate with the LIM-7 transcriptional complex." (0)

  • Overview

    Status:
    Publication type:
    Meeting_abstract
    WormBase ID:
    WBPaper00057972

    Ramadin, V., & Vallier, L. G. (2019). The search for additional proteins that physically associate with the LIM-7 transcriptional complex presented in International Worm Meeting. Unpublished information; cite only with author permission.

    The LIM-Homeodomain (LIM-HD) family of transcription factors, which are conserved throughout evolution, are characterized by the presence of two specialized zinc fingers that are located N-terminally to a DNA-binding homeodomain. LIM-HD proteins have been well studied in the context of neuronal patterning in many phyla, in addition to being present and studied in a variety of non-neuronal tissues. The Vallier lab is interested in the LIM-HD protein, LIM-7, an essential transcription factor. lim-7 is expressed in many tissues including the reproductive system, nervous system, muscular system, and alimentary system. To begin to understand the role of lim-7 in these tissues, as well as its essential role for viability, the Vallier lab has been taking a multi-prolonged approach. Currently, 25 known proteins are known to physically interact or regulate lim-7 and an equal number are predicted to interact. We are interested to see if any of these known factors are acting in a combinatorial fashion in a transcriptional complex with LIM-7 in various tissues to specify tissue identity. As a first step toward this goal, we wanted to see if any additional proteins were associating with lim-7 physically. Therefore, we attempted an affinity pull down of protein lysates using a tagged lim-7 strain, to assess the presence of proteins that were associated with it by Coomassie gels, using Western Blots for loading controls and LIM-7 presence. Preliminary attempts have shown promising results. Additional affinity pull-down experiments to optimize conditions are in progress and will be analyzed by mass spectroscopy. Results will be reported.

    Affiliation:
    - Biology, Hofstra Univ, Hempstead, NY


    Tip: Seeing your name marked red? Please help us identify you.