© 2017

Prokaryotic Chaperonins

Multiple Copies and Multitude Functions

  • C. M. Santosh Kumar
  • Shekhar C. Mande

Part of the Heat Shock Proteins book series (HESP, volume 11)

Table of contents

  1. Front Matter
    Pages i-ix
  2. Structure–Function of Chaperonins

    1. Front Matter
      Pages 1-1
    2. Sara E. Rowland, Frank T. Robb
      Pages 3-20
  3. Multiple Chaperonins of Bacterial System

    1. Front Matter
      Pages 37-37
    2. Li Zhuo, Yan Wang, Zheng Zhang, Yue-zhong Li
      Pages 53-65
    3. Hema Rajaram, Akhilesh K. Chaurasia, Akhilesh A. Potnis
      Pages 93-109
  4. Multiple Chaperonins of Archaeal System

    1. Front Matter
      Pages 111-111
    2. Le Gao, Shinsuke Fujiwara
      Pages 113-128
  5. Evolution of Multiple Copies of Chaperonins

    1. Front Matter
      Pages 147-147

About this book


​This book focuses on a topical and timely aspect of prokaryotic biology - the biology of prokaryotic multiple chaperonins. Chaperonins are a class of molecular chaperones, the proteins that assist folding of other proteins in the cell. The book begins with an introductory chapter on the structural and functional aspects of chaperonins, followed by an outline on different mechanisms of their regulation. Subsequently, the book provides a comprehensive overview on how the multiple-chaperonins have embraced biological requirements in different classes of microbes, discussing their functional diversity, evolutionary paths and the latest advances in the field.

It brings together leading experts from across the globe in offering a detailed account of the structural, biochemical, functional and phylogenetic characteristics of microbial chaperonins for students, researchers and teachers working in the area of microbiology/ biophysics/ parasitology – more specifically, in protein folding pathways. 


Molecular Chaperones Protein Folding Stress Response Moonlighting Functions Pathogenic Bacteria

Editors and affiliations

  • C. M. Santosh Kumar
    • 1
  • Shekhar C. Mande
    • 2
  1. 1.Institute of Microbiology and Infection – School of BiosciencesUniversity of BirminghamBirmingham, West MidlandsUnited Kingdom
  2. 2.Laboratory of Structural BiologyNational Centre for Cell SciencePuneIndia

About the editors

C. M. Santosh Kumar started his research career as a molecular geneticist, exploring the functions of molecular chaperones in health and disease. His research aims at understanding the functions of the bacterial chaperonins, especially those of the multiple chaperonins. He has demonstrated that activity of a mycobacterial chaperonin is regulated by a phosphorylation switch that facilitates oligomerization. His current interests include unravelling the role of mycobacterial chaperonins in the establishment and progression of tubercular disease.


Shekhar C. Mande is a structural biologist interested in understanding the molecular attributes of mycobacterial stress proteins. He started his career as a structural biologist in understanding the structural features of peanut lectin. Further, he became interested in the structure-function relations of mycobacterial stress proteins, such as the redox proteins and heat-shock proteins. He led the way towards the understanding of structural features of the mycobacterial chaperonin proteins. His work demonstrated that mycobacterial chaperonins exhibit non-canonical attributes that are evolved to assist the pathogen in its disease establishment and progression. Concurrently, he began to explore the system wide functional interactions among the mycobacterial proteins. These investigations have led to the identification of several novel interactions that are currently being examined.

Bibliographic information

Industry Sectors
Consumer Packaged Goods