Protein-protein interactions between histidine kinases and response regulators of Mycobacterium tuberculosis H37Rv

Lee, Ha-Na; Jung, Kwang-Eun; Ko, In-Jeong; Baik, Hyung; Oh, Jeong-Il
April 2012
Journal of Microbiology;Apr2012, Vol. 50 Issue 2, p270
Academic Journal
No abstract available.


Related Articles

  • A tale of two components: a novel kinase and a regulatory switch. Robinson, Victoria L.; Buckler, David R.; Stock, Ann M. // Nature Structural Biology;Aug2000, Vol. 7 Issue 8, p626 

    Histidine protein kinases and response regulators form the basis of phosphotransfer signal transduction pathways. Commonly referred to as two-component systems, these modular and adaptable signaling schemes are prevalent in prokaryotes. Structures of the core domains of histidine kinases reveal...

  • Conformational Dynamics of Response Regulator RegX3 from Mycobacterium tuberculosis. Ahmad, Ashfaq; Cai, Yongfei; Chen, Xingqiang; Shuai, Jianwei; Han, Aidong // PLoS ONE;7/22/2015, Vol. 10 Issue 7, p1 

    Two-component signal transduction systems (TCS) are vital for adaptive responses to various environmental stresses in bacteria, fungi and even plants. A TCS typically comprises of a sensor histidine kinase (SK) with its cognate response regulator (RR), which often has two domains—N...

  • Regulation of Polar Peptidoglycan Biosynthesis by Wag31 Phosphorylation in Mycobacteria. Jani, Charul; Hyungjin Eoh; Jae Jin Lee; Hamasha, Khozima; Sahana, Moodakare Bheema; Jeong-Sun Han; Nyayapathy, Seeta; Jung-Yeon Lee; Joo-Won Suh; Sang Hee Lee; Rehse, Steve J.; Crick, Dean C.; Choong-Min Kang // BMC Microbiology;2010, Vol. 10, p327 

    Background: Sensing and responding to environmental changes is a central aspect of cell division regulation. Mycobacterium tuberculosis contains eleven Ser/Thr kinases, two of which, PknA and PknB, are key signaling molecules that regulate cell division/morphology. One substrate of these kinases...

  • Host Innate Immune Response to Mycobacterium tuberculosis. Kamlesh Bhatt; Padmini Salgame // Journal of Clinical Immunology;Jul2007, Vol. 27 Issue 4, p347 

    This review focuses on recent progress in our understanding of Mycobacterium tuberculosis survival in macrophages, the interaction of M. tuberculosis with Toll-like receptors (TLRs) and the establishment of the link between innate and adaptive immunity, and TLRs and interferon-γ-mediated...

  • In silico prediction of protein-protein interactions in human macrophages. Souiai, Oussema; Guerfali, Fatma; Ben Miled, Slimane; Brun, Christine; Benkahla, Alia // BMC Research Notes;2014, Vol. 7 Issue 1, p157 

    Background: Protein-protein interaction (PPI) network analyses are highly valuable in deciphering and understanding the intricate organisation of cellular functions. Nevertheless, the majority of available protein-protein interaction networks are context-less, i.e. without any reference to the...

  • Searching for Potential Drug Targets in Two-component and Phosphorelay Signal-transduction Systems using Three-dimensional Cluster Analysis. Cai, Xiao-Hui; Zhang, Qing; Shi, Shuo-Yong; Ding, Da-Fu // Acta Biochimica et Biophysica Sinica;May2005, Vol. 37 Issue 5, p293 

    Two-component and phosphorelay signal transduction systems are central components in the virulence and antimicrobial resistance responses of a number of bacterial and fungal pathogens; in some cases, these systems are essential for bacterial growth and viability. Herein, we analyze in detail the...

  • Two-Component Signal Transduction Pathways Regulating Growth and Cell Cycle Progression in a Bacterium: A System-Level Analysis. Skerker, Jeffrey M.; Prasol, Melanie S.; Perchuk, Barrett S.; Biondi, Emanuele G.; Laub, Michael T. // PLoS Biology;Oct2005, Vol. 3 Issue 10, p1770 

    Two-component signal transduction systems, comprised of histidine kinases and their response regulator substrates, are the predominant means by which bacteria sense and respond to extracellular signals. These systems allow cells to adapt to prevailing conditions by modifying cellular...

  • Letter to the Editor: 1H, 13C and 15N resonance assignment and secondary structure of Mycobacterium tuberculosis adenylate kinase. Miron, Simona; Munier-Lehmann, Hélène; Craescu, Constantin T. // Journal of Biomolecular NMR;Jan2001, Vol. 19 Issue 1, p89 

    Presents a letter to the editor about molecular structure of Mycobacterium tuberculosis adenylate kinase.

  • SpaK/SpaR Two-component System Characterized by a Structure-driven Domain-fusion Method and in Vitro Phosphorylation Studies. Chakicherla, Anu; Ecale Zhou, Carol L.; Dang, Martha Ligon; Rodriguez, Virginia; Hansen, J. Norman; Zemla, Adam // PLoS Computational Biology;Jun2009, Vol. 5 Issue 6, p1 

    Here we introduce a quantitative structure-driven computational domain-fusion method, which we used to predict the structures of proteins believed to be involved in regulation of the subtilin pathway in Bacillus subtilis, and used to predict a protein-protein complex formed by interaction...

  • Novel Role of Phosphorylation-Dependent Interaction between FtsZ and FipA in Mycobacterial Cell Division. Sureka, Kamakshi; Hossain, Tofajjen; Mukherjee, Partha; Chatterjee, Paramita; Datta, Pratik; Kundu, Manikuntala; Basu, Joyoti // PLoS ONE;2010, Vol. 5 Issue 1, p1 

    The bacterial divisome is a multiprotein complex. Specific protein-protein interactions specify whether cell division occurs optimally, or whether division is arrested. Little is known about these protein-protein interactions and their regulation in mycobacteria. We have investigated the...


Read the Article


Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics