Expression and purification of the recombinant full-length retinoblastoma protein and characterisation of its interaction with the oncoprotein HDM2
Retinoblastoma (Rb) was the first tumour suppressor factor described, and it is dysfunctional in several types of cancers. Structurally, Rb is a very large, multifunctional protein organized in different domains connected by intrinsically disordered regions. Due to the complex structure of Rb, bioch...
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| Published in: | Protein expression and purification Vol. 162; pp. 62 - 66 |
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| Abstract | Retinoblastoma (Rb) was the first tumour suppressor factor described, and it is dysfunctional in several types of cancers. Structurally, Rb is a very large, multifunctional protein organized in different domains connected by intrinsically disordered regions. Due to the complex structure of Rb, biochemical manipulation is difficult. The Rb protein has been implicated in many different cellular processes, such as the cell cycle control, senescence and even apoptosis. The activity of Rb is regulated by phosphorylation, and many different sites of phosphorylation have been described. However, the oncoprotein HDM2, can promote Rb degradation by the proteasome. This form of Rb regulation is largely unknown. Here we report the expression and purification of the full-length Rb protein and its phosphomimetic form, Rb(S567D), in a recombinant system. We also produced and purified the HDM2 protein and its phosphomimetic mutant, HDM2(S395D). The proteins interacted strongly when we used the phosphomimetic mutants, mimicking damaged DNA conditions. The expression of the proteins in E. coli allowed us to control the phosphorylation status of the proteins. |
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| AbstractList | Retinoblastoma (Rb) was the first tumour suppressor factor described, and it is dysfunctional in several types of cancers. Structurally, Rb is a very large, multifunctional protein organized in different domains connected by intrinsically disordered regions. Due to the complex structure of Rb, biochemical manipulation is difficult. The Rb protein has been implicated in many different cellular processes, such as the cell cycle control, senescence and even apoptosis. The activity of Rb is regulated by phosphorylation, and many different sites of phosphorylation have been described. However, the oncoprotein HDM2, can promote Rb degradation by the proteasome. This form of Rb regulation is largely unknown. Here we report the expression and purification of the full-length Rb protein and its phosphomimetic form, Rb(S567D), in a recombinant system. We also produced and purified the HDM2 protein and its phosphomimetic mutant, HDM2(S395D). The proteins interacted strongly when we used the phosphomimetic mutants, mimicking damaged DNA conditions. The expression of the proteins in E. coli allowed us to control the phosphorylation status of the proteins. |
| Author | Rousset-Roman, Adriana Olivares-Illana, Vanesa Rebolloso-Gómez, Yolanda |
| Author_xml | – sequence: 1 givenname: Adriana surname: Rousset-Roman fullname: Rousset-Roman, Adriana – sequence: 2 givenname: Yolanda surname: Rebolloso-Gómez fullname: Rebolloso-Gómez, Yolanda – sequence: 3 givenname: Vanesa surname: Olivares-Illana fullname: Olivares-Illana, Vanesa email: vanesa@ifisica.uaslp.mx |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/31163228$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_15252_embr_202050615 crossref_primary_10_3390_cancers14051265 crossref_primary_10_3389_fonc_2021_777867 |
| Cites_doi | 10.1101/gad.1590607 10.1101/gad.886901 10.1101/SQB.1991.056.01.020 10.1111/apm.12274 10.1016/0092-8674(95)90385-2 10.1016/j.tibs.2012.10.007 10.1038/sj.onc.1204337 10.1016/S0165-4608(96)00395-0 10.1073/pnas.0436813100 10.1038/375694a0 10.1016/j.molcel.2016.08.015 10.1038/323643a0 10.1038/nrc2763 10.4161/cc.5.5.2515 10.1016/0092-8674(91)90557-F 10.1038/nrm3567 10.1038/onc.2016.32 10.1038/nrc2718 10.4161/cc.8.1.7326 10.1038/ncb1770 10.1038/sj.emboj.7601668 10.1038/onc.2010.442 10.1128/MCB.00113-16 10.1016/j.ccr.2011.11.016 10.1074/jbc.M406062200 10.1016/j.molcel.2005.10.017 10.1101/gad.211326.112 10.1038/sj.emboj.7600486 |
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| Keywords | Retinoblastoma protein protein:protein interactions Purification |
| Language | English |
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| Snippet | Retinoblastoma (Rb) was the first tumour suppressor factor described, and it is dysfunctional in several types of cancers. Structurally, Rb is a very large,... |
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| StartPage | 62 |
| SubjectTerms | protein:protein interactions Purification Retinoblastoma protein |
| Title | Expression and purification of the recombinant full-length retinoblastoma protein and characterisation of its interaction with the oncoprotein HDM2 |
| URI | https://dx.doi.org/10.1016/j.pep.2019.05.011 https://www.ncbi.nlm.nih.gov/pubmed/31163228 https://search.proquest.com/docview/2243485431 |
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