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Title: Molecular interaction between human SUMO-I and histone like DNA binding protein of Helicobacter pylori (Hup) investigated by NMR and other biophysical tools
Authors: Jaiswal N.
Agarwal N.
Kaur A.
Tripathy S.
Gahlay G.K.
Arora A.
Mitthu V.S.
Poluri, Krishna Mohan
Kumar D.
Published in: International Journal of Biological Macromolecules
Abstract: The proteins secreted by bacteria contribute to immune mediated gastric inflammation and epithelial damage; thus aid bacterial invasion in host tissue, and may also interact with host proteins, conspirating a mechanism against host-immune system. The Histone-like DNA binding protein is one of the most abundant nucleoid-associated proteins in Helicobacter pylori (H. pylori). The protein –referred here as Hup- is also secreted in vitro by H. pylori, thus it may have its role in disease pathogenesis. This is possible only if Hup interact with some human proteins including Small-Ubiquitin-like-Modifier (SUMO) proteins. Studies have established that SUMO-proteins participate in various innate-immune pathways and thus promote an efficient immune response to combat pathogenic infections. Sequence analysis revealed the presence of two SUMO interacting motifs (SIMs) and several positively charged lysine residues on the protein surface of Hup. Additionally, SUMO-proteins epitomize negatively charged surface which confers them the ability to bind to DNA/RNA binding proteins. Based on the presence of SIMs as well as charge complementarity between the proteins, it is legitimate to consider that Hup protein would bind to SUMO-proteins. The present study has been undertaken to establish this interaction for the first time using NMR in combination with ITC and other biophysical techniques. © 2018
Citation: International Journal of Biological Macromolecules(2019), 123(): 446-456
Issue Date: 2019
Publisher: Elsevier B.V.
Keywords: Helicobacter pylori
Histone like DNA binding protein
Human SUMO-1
Hup-SUMO-1 interaction
Small Ubiquitin like Modifier
SUMO interacting motifs
ISSN: 1418130
Author Scopus IDs: 57193557431
Author Affiliations: Jaiswal, N., Centre of Biomedical Research, SGPGIMS Campus, Lucknow, 226014, India, Dr. APJ Abdul Kalam Technical University, IET Campus, Sitapur Road, Lucknow, Uttar Pradesh 226031, India
Agarwal, N., Department of Biotechnology, Centre for Nanotechno
Funding Details: We thank the Government of India for providing financial support to the National Facility for High Field NMR at the CBMR, Lucknow. DK and KMP would also like to acknowledge SERB DST, India for providing the research grant under EMR Scheme (Registration Nu
Corresponding Author: Kumar, D.; Centre of Biomedical Research, SGPGIMS CampusIndia; email:
Appears in Collections:Journal Publications [BT]

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