RESEARCH COMMUNICATION

Experimental Help!

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  • ravi

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  • RAMESH

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  • RAMESH

Experimental Help!

I have a question regarding my experiment! In of the project, I am studying the role of individual lysine residue in the target protein (X) ubiquitination. I am using WT Ubiquitin, and K0 (all seven lysine of the Ubiquitin protein is mutated) plasmid DNA constructs. To understand the residue specificity, I have mutated K>R individually and generated seven new plasmid DNA. After the experiment, I can see loss of protein X ubiquitination only in K0 mutant and none of these individual sites display any defect. My question is 1. Why don't I see any defect with the mutant plasmid DNA construct. 2. Does is mean that many K sites are required for this? 3. What is best possible experimental approach to address this. Thanks!

  • RAMESH

Need expert opinion!

I have a question regarding my experiment! In of the project, I am studying the role of individual lysine residue in the target protein (X) ubiquitination. I am using WT Ubiquitin, and K0 (all seven lysine of the Ubiquitin protein is mutated) plasmid DNA constructs. To understand the residue specificity, I have mutated K>R individually and generated seven new plasmid DNA. After the experiment, I can see loss of protein X ubiquitination only in K0 mutant and none of these individual sites display any defect. My question is 1. Why don't I see any defect with the mutant plasmid DNA construct. 2. Does is mean that many K sites are required for this? 3. What is best possible experimental approach to address this. Thanks!

  • RAMESH

IF YOUR QUERY IS NOT FITTING WITH ABOVE 5 SECTIONS

hi

  • RAMESH

Need expert opinion!

Role of MDM2 and other E3 ligases in the ubiquitination of p53 has been deeply investigated. MDM2 and p53 binding is well defined. I am interested to know whether p53 hotspot mutations either effect the MDM-p53 interaction or the ability of mutant p53 for K48-likned poly-ubiquitination. Other possibility would be only specific structurally distorted mutants are neutral for MDM2 action. A list of p53 mutants, which can still bind to the MDM2 and normally ubiquitinated. Similarly a list of mutant which can not bind to mutant p53 and its ubiquitination. I am searching for paper and/or review article which can provide me detail information of MDM2-mutant p53 interaction and Ubiquitination.

  • RAMESH

Need expert opinion!

Role of MDM2 and other E3 ligases in the ubiquitination of p53 has been deeply investigated. MDM2 and p53 binding is well defined. I am interested to know whether p53 hotspot mutations either effect the MDM-p53 interaction or the ability of mutant p53 for K48-likned poly-ubiquitination. Other possibility would be only specific structurally distorted mutants are neutral for MDM2 action. A list of p53 mutants, which can still bind to the MDM2 and normally ubiquitinated. Similarly a list of mutant which can not bind to mutant p53 and its ubiquitination. I am searching for paper and/or review article which can provide me detail information of MDM2-mutant p53 interaction and Ubiquitination.

  • RAMESH