Investigation of protein-protein interactions involving Retinoblastoma Binding Protein 6 using immunoprecipitation and Nuclear Magnetic Resonance Spectroscopy
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Date
2019
Authors
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Journal ISSN
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Publisher
University of the Western Cape
Abstract
Retinoblastoma Binding Protein 6 (RBBP6) is a 200 KDa multi-domain protein that has been
shown to play a role in mRNA processing, cell cycle arrest and apoptosis. RBBP6 interacts with
tumour suppressor proteins such as p53 and pRb and has been shown cooperate with Murine
Double Minute 2 (MDM2) protein in catalyzing ubiquitination and suppression of p53.
Unpublished data from our laboratory has suggested that RBBP6 and MDM2 interact with each
other through their RING finger domains. RBBP6 has also been shown to have its own E3 ubiquitin
ligase activity, catalyzing ubiquitination of Y-Box Binding Protein 1 (YB-1) in vitro and in vivo. YB-
1 is a multifunctional oncogenic protein that is generally associated with poor prognosis in cancer,
tumourigenesis, metastasis and chemotherapeutic resistance. Unpublished data from our
laboratory shows that RBBP6 catalyzes poly-ubiquitination of YB-1, using Ubiquitin-conjugating
enzyme H1 (UbcH1) as E2 ubiquitin conjugating enzyme. We have furthermore shown that the
zinc knuckle of RBBP6 interacts specifically with the Ubiquitin-associated domain (UBA) domain
of UbcH1.
Description
>Magister Scientiae - MSc
Keywords
Immunoprecipitation, Protein, Tumour Suppressor