Oligomerization of THAP9 transposase via amino-terminal domains

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dc.contributor.author Sanghavi, Hiral M.
dc.contributor.author Majumdar, Sharmistha
dc.coverage.spatial United States of America
dc.date.accessioned 2021-06-05T09:32:51Z
dc.date.available 2021-06-05T09:32:51Z
dc.date.issued 2021-05
dc.identifier.citation Sanghavi, Hiral M. and Majumdar, Sharmistha, “Oligomerization of THAP9 transposase via amino-terminal domains”, Biochemistry, DOI: 10.1021/acs.biochem.1c00010, vol. 60, no. 23, pp. 1822-1835, Jun. 2021. en_US
dc.identifier.issn 0006-2960
dc.identifier.issn 1520-4995
dc.identifier.uri https://doi.org/10.1021/acs.biochem.1c00010
dc.identifier.uri https://repository.iitgn.ac.in/handle/123456789/6548
dc.description.abstract Active DNA transposases like the Drosophila P element transposase (DmTNP) undergo oligomerization as a prerequisite for transposition. Human THAP9 (hTHAP9) is a catalytically active but functionally uncharacterized homologue of DmTNP. Here we report (using co-immunoprecipitation, pull down, colocalization, and proximity ligation assays) that both full length and truncated hTHAP9 (corresponding to amino-terminal DNA binding and predicted coiled coil domains) undergo homo-oligomerization, predominantly in the nuclei of HEK293T cells. Interestingly, the oligomerization is shown to be partially mediated by DNA. However, mutating the leucines (either individually or together) or deleting the predicted coiled coil region did not significantly affect oligomerization. Thus, we highlight the importance of DNA and the amino-terminal regions of hTHAP9 for their ability to form higher-order oligomeric states. We also report that Hcf-1, THAP1, THAP10, and THAP11 are possible protein interaction partners of hTHAP9. Elucidating the functional relevance of the different putative oligomeric state(s) of hTHAP9 would help answer questions about its interaction partners as well as its unknown physiological roles.
dc.description.statementofresponsibility by Hiral M. Sanghavi and Sharmistha Majumdar
dc.format.extent vol. 60, no. 23, pp. 1822-1835
dc.language.iso en_US en_US
dc.publisher American Chemical Society en_US
dc.subject Immunology en_US
dc.subject Peptides and proteins en_US
dc.subject Genetics en_US
dc.subject Oligomerization en_US
dc.subject Biopolymers en_US
dc.title Oligomerization of THAP9 transposase via amino-terminal domains en_US
dc.type Article en_US
dc.relation.journal Biochemistry

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