Protein Adaptation in Extremophiles

Front Cover
Nova Publishers, 2008 - Science - 250 pages
Life has evolved in an extraordinary way to deal with the most extreme physical and chemical conditions. Extremophilic (extreme-loving) organisms have been found in the superheated waters of deep ocean vents or the hypersaline and cold lakes of Antarctica and indeed often require the extreme conditions of their habitat to survive and thrive. The cellular machinery of extremophiles has developed unique adaptation strategies to effectively function in their given environment. Much scientific attention has focussed on the adaptation of proteins as they have both structural and catalytic functions and hence play key roles in all cellular processes. Moreover, their ability to perform in or withstand extreme physical and chemical conditions has made extremophilic proteins attractive bio-catalysts for a range of industrial and biotechnological applications. This novel and significant book comprehensively summarises our current understanding regarding the structure-function-stability relationship of extremophilic proteins. Leading experts in the field extensively review and comment on the adaptation of proteins to the whole spectrum of physical and chemical extremes. This book represents an important and indispensable reference for students, teachers and researchers with interest or activities in the fascinating area of extremophiles.

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Comments on book by George Somero, David & Lucile Packard Professor in Marine Sciences, Biochemical Adaptation, Evolution & Ecological Physiology, Associate Director of Hopkins Marine Station, Stanford, USA.
I greatly enjoyed and benefited from reading this volume (Protein Adaptation in Extremophiles). With the possible exception of the final chapter, the book contained material of relevance to my teaching as well as my research. I plan to assign some of these chapters for the students in my spring term class on biochemical adaptation.
In the most general sense, I appreciated three principal things about this book. One (obviously) was the broad coverage given to the subject, such that all of the relevant environmental factors, both chemical and physical, that affect protein structure and function were examined. I don't know of another volume that has this comprehensive coverage of protein adaptation between its covers. The second characteristic of the book that I found useful (speaking here as someone who's primarily focused on animals!) was the comprehensive treatment of the literature on bacterial and archaeal proteins. Some of this literature was easy for someone (like me) to miss who does not effectively sift through such sources as symposium volumes.
The third thing I appreciated (and here I'm thinking of how useful the volume will be for teaching) was the authors efforts to communicate their subject matter in manners that make the work accessible to the non-specialist. The first chapter by Daniel et al. exemplifies this approach. The authors have written one of the clearest, yet nicely detailed accounts of protein thermal stability that I have read. It reminded me very much of the approach used by John Brandts in his classic 1967 review in "Thermobiology," in which a sophisticated and advanced analysis is developed in a way that even a relative newcomer to the topic could follow. In the Daniel et al. chapter I really appreciated being given the relevant abbreviations for the "Two-State" and "Equilibrium" models right at the beginning of the chapter. This foundational information, in conjunction with the clear explanatory figures (numbers 1-3) that were used to introduce the topic, will give the reader a solid foundation on which to build understanding of the more detailed elements in the chapter. Their Equilibrium Model is a fascinating and powerful one that, thanks to this chapter, will be appreciated by a broader set of investigators and students. The explanation of how temperature affects rates of enzymatic activity was one of the clearest I have read. Very "student friendly" writing.
The chapter by Georges Feller on low-temperature effects is a good complement to the analysis in the Daniel et al. chapter on high-temperature effects. Feller writes beautifully, and I will be using this chapter in my class to provide students with an especially good entry into low-temperature adaptation of proteins. Like Daniel et al., Feller presents figures that have text-book clarity and make their points unambiguously. Feller does an especially good job of writing a broadly applicable analysis, one that includes prokaryotes and eukaryotes in its focus. The literature review is very well done.
The analysis of halophilic proteins given by Bolhuis et al. in Chapter III has a broad focus that emphasize the "cooperative" effort between proteins and the osmotic solutes of the cell in sustaining protein structure and function under extremely high osmolalities. As in the other chapters, the references led me to look at literature I had missed. I greatly appreciated the information provided on the costs of producing compatible solutes in halophilic species. This was a piece of the puzzle I had not seen discussed before.
The chapter on "Alkaline Adaptation of Proteins" by Shirai et al. contained material that was mostly new to me. The writing was a good introduction to this subject. I liked the treatment given to how pKa


Enzyme Stability and Activity at High Temperatures
Enzyme Function at Low Temperatures in Psychrophiles
Halophilic Adaptations of Proteins
Alkaline Adaptation of Proteins
Thermoacidophiles and their Protein Adaptation to Low pH and High Temperature
Protein Adaptation to HighPressure Environments
Organic SolventStable Enzymes

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