In vitro assembly complex formation of TRAIP CC and RAP 80 zinc finger motif revealed by our study

Background: Tumor necrosis factor interacting protein (TRAIP/TRIP) is an important cell-signaling molecule that prevents the TNF-induced-nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) activation via direct interaction with TRAF 2 protein. TRAIP is a crucial downstream signali...

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Autores principales:	Eijaz Ahmed Bhat, Nasreena Sajjad, Irfan A. Rather, Jamal S.M. Sabir, Yan-Yan Hor
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	TNF-protein RAP- 80 Protein interaction NF-kB Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/e687aab6abb849128cfd3e04189bf8fc
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spelling	oai:doaj.org-article:e687aab6abb849128cfd3e04189bf8fc2021-11-20T04:57:16ZIn vitro assembly complex formation of TRAIP CC and RAP 80 zinc finger motif revealed by our study1319-562X10.1016/j.sjbs.2021.08.083https://doaj.org/article/e687aab6abb849128cfd3e04189bf8fc2021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S1319562X21007713https://doaj.org/toc/1319-562XBackground: Tumor necrosis factor interacting protein (TRAIP/TRIP) is an important cell-signaling molecule that prevents the TNF-induced-nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) activation via direct interaction with TRAF 2 protein. TRAIP is a crucial downstream signaling molecule, implicated in several signaling pathways. Due to these multifunctional effects, TRAIP is more related to cellular mitosis, chromosome segregation, and DNA damage response. Tumor necrosis factor interacting protein is a downstream signaling molecule that contains a RING domain with E3 ubiquitin ligase activity at the N terminal side followed by coiled-coil and C terminal leucine zipper domain. Human TRAIP is constituted of 469 amino acids with 76% sequence similarity with the mouse TRAIP protein. Although, the main inhibitory function of TRAIP has been known for decades, however, in vitro interaction of TRAIPCC domain with RAP80 Zinc finger motif has not been reported yet. Besides, RAP80, the binding partner of TRAIPCC protein has been implicated in DNA damage response. Results: Our in vitro study shows that the TRAIP CC (64–166) associates with the RAP80 zinc finger of corresponding amino acid 490–584. However, TRAIP CCLZ (66–260) and TRAIP RINGCC (1 = 157) failed to interact with the RAP80 zinc finger of corresponding amino acid 490–584. The current study reinforces TRAIP CC (64–166) and RAP80 zinc finger of corresponding amino acid 490–584 associates to form a complex. Moreover, SDS PAGE arbitrated the homogeneity of RAP80 Zinc finger and TRAIP CC of corresponding amino acid 490–584 and 64–166, respectively. Conclusion: In vitro, a specific interaction was observed between the TRAIP CC (64–166) and the RAP80 zinc finger of the corresponding amino acid 490–584 and a specific binding area of the RAP80 zinc finger motif were investigated. The TRAIPCC region is required for the complex to bind to the RAP80-Zn finger motif. This strategy may be necessary for the RAP80 zinc finger activity to the TRAIP CC protein.Eijaz Ahmed BhatNasreena SajjadIrfan A. RatherJamal S.M. SabirYan-Yan HorElsevierarticleTNF-proteinRAP- 80Protein interactionNF-kBBiology (General)QH301-705.5ENSaudi Journal of Biological Sciences, Vol 28, Iss 12, Pp 7511-7516 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	TNF-protein RAP- 80 Protein interaction NF-kB Biology (General) QH301-705.5
spellingShingle	TNF-protein RAP- 80 Protein interaction NF-kB Biology (General) QH301-705.5 Eijaz Ahmed Bhat Nasreena Sajjad Irfan A. Rather Jamal S.M. Sabir Yan-Yan Hor In vitro assembly complex formation of TRAIP CC and RAP 80 zinc finger motif revealed by our study
description	Background: Tumor necrosis factor interacting protein (TRAIP/TRIP) is an important cell-signaling molecule that prevents the TNF-induced-nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) activation via direct interaction with TRAF 2 protein. TRAIP is a crucial downstream signaling molecule, implicated in several signaling pathways. Due to these multifunctional effects, TRAIP is more related to cellular mitosis, chromosome segregation, and DNA damage response. Tumor necrosis factor interacting protein is a downstream signaling molecule that contains a RING domain with E3 ubiquitin ligase activity at the N terminal side followed by coiled-coil and C terminal leucine zipper domain. Human TRAIP is constituted of 469 amino acids with 76% sequence similarity with the mouse TRAIP protein. Although, the main inhibitory function of TRAIP has been known for decades, however, in vitro interaction of TRAIPCC domain with RAP80 Zinc finger motif has not been reported yet. Besides, RAP80, the binding partner of TRAIPCC protein has been implicated in DNA damage response. Results: Our in vitro study shows that the TRAIP CC (64–166) associates with the RAP80 zinc finger of corresponding amino acid 490–584. However, TRAIP CCLZ (66–260) and TRAIP RINGCC (1 = 157) failed to interact with the RAP80 zinc finger of corresponding amino acid 490–584. The current study reinforces TRAIP CC (64–166) and RAP80 zinc finger of corresponding amino acid 490–584 associates to form a complex. Moreover, SDS PAGE arbitrated the homogeneity of RAP80 Zinc finger and TRAIP CC of corresponding amino acid 490–584 and 64–166, respectively. Conclusion: In vitro, a specific interaction was observed between the TRAIP CC (64–166) and the RAP80 zinc finger of the corresponding amino acid 490–584 and a specific binding area of the RAP80 zinc finger motif were investigated. The TRAIPCC region is required for the complex to bind to the RAP80-Zn finger motif. This strategy may be necessary for the RAP80 zinc finger activity to the TRAIP CC protein.
format	article
author	Eijaz Ahmed Bhat Nasreena Sajjad Irfan A. Rather Jamal S.M. Sabir Yan-Yan Hor
author_facet	Eijaz Ahmed Bhat Nasreena Sajjad Irfan A. Rather Jamal S.M. Sabir Yan-Yan Hor
author_sort	Eijaz Ahmed Bhat
title	In vitro assembly complex formation of TRAIP CC and RAP 80 zinc finger motif revealed by our study
title_short	In vitro assembly complex formation of TRAIP CC and RAP 80 zinc finger motif revealed by our study
title_full	In vitro assembly complex formation of TRAIP CC and RAP 80 zinc finger motif revealed by our study
title_fullStr	In vitro assembly complex formation of TRAIP CC and RAP 80 zinc finger motif revealed by our study
title_full_unstemmed	In vitro assembly complex formation of TRAIP CC and RAP 80 zinc finger motif revealed by our study
title_sort	in vitro assembly complex formation of traip cc and rap 80 zinc finger motif revealed by our study
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/e687aab6abb849128cfd3e04189bf8fc
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In vitro assembly complex formation of TRAIP CC and RAP 80 zinc finger motif revealed by our study

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