Thermostability, the summary
Ronald Knegtel
ronald at rugcbf.chem.rug.nl
Wed Jul 12 10:55:01 EST 1995
Dear netters,
as requested I send you a summary of the replies I got.
An interesting review by A. Fontana (How nature engineers protein
(thermo) stability) in "Life under extreme conditions" Springer
Verlag Berlin Heidelberg 1991, Guido di Prisco (Ed.), pp. 89-113.
As for the rest of the responses...it's quite a long list
Here we go:
Look up Chan et al. (1995).Structure of a hyperthemophilic
tunstopterin enzyme, ferredoxin oxidoreductase. Science 267:1463-1469.
Would you please send a summary of the answers you get to this mailing
list. Since I am also working on a thermophilic enzyme I would be
interested in that.
Regards,
Menachem Shoham
Case Western Reserve University
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We are also working on a protein from an extreme thermophile which
likes to grow at 87C. We have just solved the structure, and the
first obvious thing is the presence of a lot of salt-bridges
criss-crossing the protein surface. This phenomenon has been
noted previously by Mike Danson and Garry Taylor at the
University of Bath. I know Mike Danson has given a lot of talks
about protein thermostability, but I dont know if he has written any
reviews. You could just look his name up on Medline or some other
computer bibliography system.
&
My physical chemistry friends (I have one or two, but they are sad creatures)
tell me that the free energy difference between a protein that denatures at 45
degrees and a protein that denatures at 95 degrees is only a few Kcal/mole,
equivalent to one or two hydrogen bonds !! If that really is he case, we will
all go very mad trying to understand thermostability.
Much more interesting is thermophilicity which is a common property of enzymes
from extreme and hyper (>100 degrees) thermophiles. This means that the enzyme
doesn't work until it reaches the high temperature !. I think this is quite
different from moderate thermophiles such B.stearothermophilus etc.
Presumably the enzyme is very rigid at normal temperatures, but it isn't clear
whether the greater rate at the higher optimal temperature is due to easier
substrate binding in a more flexible active site, or to better chemical
catalysis. The other thing that worries me is how specificity is maintained at
very high temperatures.
There is a good thermophile protein meeting in London this Autumn. If you are
interested I will try and find the details.
Laurence Pearl
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The reference is:
The crystal structure of citrate synthase from the
thermophilic archaeon, Thermoplasma
acidophilum.
Russell RJ; Hough DW; Danson MJ; Taylor GL
School of biology and Biochemistry, University of Bath, UK.
Structure 2: 1157-67 (1994)
Some other references I got from medline and which seemed interesting:
Nature 324, 695-7 (1986)
Proteins 5:22-37, 1989
Protein Eng. 1:477-80 (1987)
" " 4:11-33 (1990)
" " 165-70 (1992)
Biochemistry 32: 3913-22 (1993)
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recent: dc rees & mww adams, structure 3, 251-254 (1995)
not-so-recent, but several references to earlier work
are in: gj davies et al, proteins 15, 283-289 (1993)
--gerard kleijwegt
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i've done a bit of reading on that topic since i have once been interested
in GAPDH from thermotoga maritima. actually i'm still interested, but
maybe a bit more confused now. i'll give you a list of articles i have looked
at. it's not complete, but maybe you'll find something usefull. i'll leave
it up to you to sort yourself through this. have fun !
ingo
@article{ADWW_88_42 ,
author = { T. Alber and S. Dao-pin and K. Wilson and J.A. Woznia
k and S.P. Cook and B.W. Matthews },
title = { Contribution of hydrogen bonds of Thr 157 to the thermo
dynamic stability of phage T4 lysozyme.},
year = 1988,
journal = { Nature ( London )},
volume = { 330},
pages = { 42--46 }}
@article{BHTW_77_328 ,
author = { G. Biesecker and J.I. Harris and J.C. Thierry and J.E.
Walker and A.J. Wonacott },
title = { Sequences and structure of D-glyceraldehyde-3-phosphate
dehydrogenase from \textit{Bacillus stearothermophilus} .},
year = 1977,
journal = { Nature ( London )},
volume = { 266 },
pages = { 328--333 }}
@article{DBM_90_198 ,
author = { S. Dao-pin and W.A. Baase and B.W. Matthews },
title = { A mutant T4 lysozyme ( Val 131 -> Ala ) designed to
increase thermostability by the reduction of strain within
an
$\alpha$ helix },
year = 1990,
journal = { Proteins : Struct. Funct. Genet.},
volume = { 7 },
pages = { 198--204 }}
@article{IKKM_93_85,
author = { K. Ishikawa and S. Kimura and S. Kanaya and K. Morika
wa and H. Nakamura },
title = { Structural study of mutants of \textit{ Escherichia
coli} ribonuclease {HI} with enhanced thermostability.},
year = 1993,
journal = { Protein Engineering },
volume = { 6 },
pages = { 85--91 }}
@article{LKGJ_92_769 ,
author = { A. Luyten and C.M. Kay and M. Gold and J.B. Jones },
title = { Single amino acid substitutions can further increase
thee stability of a thermophilic L-lactate dehydrogenase.},
year = 1992,
journal = { Protein Engineering},
volume = { 5 },
pages = { 769--774 }}
@article{KNOB_93_3913 ,
author = { C.A. Kelly and M. Nishiyama and Y. Ohnishi and
T. Beppu and J.J. Birktoft },
title = { Determinants of protein stability in the 1.9-{\AA} crystal
structure of malate dehydrogenase from the thermophilic
bacterium \textit{Thermus f\/lavus} },
year = 1993,
journal = { Biochemistry },
volume = { 32 },
pages = { 3913--3922 }}
@article{NADM_91_9816 ,
author = { H. Nicholson and P.E. Anderson and S. Dao-pin and B.W.
Matthews },
title = { Analysis of interactions between charged side chains
and the $\alpha$-helix dipole using designed thermostable
mutants of phage {T}4 lysozyme },
year = 1991,
volume = { 30 },
journal = { Biochemistry },
pages = { 9816--9828 }}
@article{NHON_78_33 ,
author = { H. Nojima and K. Hon-nami and T. Oshima and H. Noda },
title = { Reversible thermal unfolding of thermostable cytochrome
c-552.},
year = 1978,
journal = { J. Mol. Biol.},
volume = { 122 },
pages = { 33--42 }}
@article{RJ_92_10999 ,
author = { V. Rehaber and R. Jaenicke },
title = { Stability and reconstitution of
{d}-Glyceraldehyde-3-phosphate dehydrogenase from
the hyperthermophilic bacterium
\textit{{T}hermotoga maritima} },
year = 1992,
journal = { J. Biol. Chem.},
volume = { 267},
pages = { 10999--11006 }}
@article{WSSJ_90_7584 ,
author = { A. Wrba and A. Schweiger and V. Schultes and
R. Jaenicke and P. Zavodsky },
title = { Extremely thermostable {D}-glyceraldehyde-3-phosphate
dehydrogenase from the eubacterium
\textit{{T}hermotoga maritima} .},
year = 1990,
journal = { Biochemistry },
volume = { 29 },
pages = { 7584--7592 }}
@article{ADWW_87_42,
author = { T. Alber and S. Dao-pin and K. Wilson and
J.A. Wozniak and S.P. Cook and B.W. Matthews },
year = 1987,
title = { Contribution of hydrogen bonds of {T}hr 157 to the
thermodynamic stability of phage {T}4 lysozyme. },
journal = { Nature (London) },
volume = 330,
pages = { 41 -- 46 } }
@article{DBM_90_198,
author = { S. Dao-pin and W.A. Baase and B.W. Matthews },
year = 1990,
title = { A mutant {T}4 lysozyme ({V}al 131 . {A}la) designed
to increase thermostability by the reduction of strain
within an $\alpha$-helix. },
journal = { Proteins : Struct. Funct. Genet. },
volume = 7,
pages = { 198 -- 204 } }
@inproceedings{HC_76,
author = { Herbert and Codd },
title = { Role of calcium ions in the thermostability of amylase
produced by \textit{{B}ac. stearothermophilus}. },
booktitle = { Proceedings of the international symposium on enzymes
and proteins from thermophilic microorganisms, Z"urich.
Structure and function. },
year = { 1976 },
editor = { Zuber, H. },
publisher = { Birkhaeuser },
address = { Basel }}
@article{KSPM_92_769,
author = { H.K.W. Kallwass and W.K. Surewicz and W. Parris and
L.A. Macfarlane and A. Luyten and C.M. Kay and
M. Gold and J.B. Jones },
year = 1992,
title = { Single amino acid substitutions can further increase
the stability of a thermophilic {L}-lactate dehydrogenase. },
journal = { Protein Engineering },
volume = 5,
pages = { 769 -- 774 } }
@article{MKIA_84_413,
author = { Matsumura, M. and Katamura, Y. and Iwanaka, T. and Aiba, S. },
year = 1984,
title = { Enzymatic and nucleotide sequence studies of a kanamycine
inactivating enzyme encoded by a plasmid from thermophilic
bacilli in comparison with that enzyme encoded by plasmid
pUB110 },
journal = { J. Bacteriol. },
volume = 160,
pages = { 413 -- ??? } }
@article{WH_74_3215,
author = { Wedler, F.C. and Hof\/fmann, F.M. },
year = 1974 ,
title = { Glutaminesynthase of \textit{Bacillus stearothermophilus}.
{II}. Regulation and thermostability },
journal = { Biochemistry },
volume = 13 ,
pages = { 3215 -- 3221 } }
@article{WSSJ_90_195,
author = { Wrba, A. and Jaenicke, R. and Huber, R. and Stetter, K.O. },
year = 1990,
title = { Lactate dehydrogenase from the extreme thermophile
\textit{Thermotoga maritima}.},
journal = { Eur. Journ. Biochem. },
volume = { 188 },
pages = { 195 -- 201}}
@article{Y_76_91,
author = { K. Yutani},
year = 1976,
title = { Role of calcium ion in the thermostability of alpha amylase
produced from \textit{Bacillus stearothermophilus}. },
journal = { Experientia },
volume = { 26 },
pages = { 91 -- 103 }}
@article{KSHT_95_511,
author = { I. Kornd"orfer and B. Steipe and R. Huber and A. Tomschy
and R. Jaenicke },
year = 1995,
title = { The crystal structure of holo-glyceraldehyde-3-phosphate
dehydrogenase from the hyperthermophilic {B}acterium
\textit{Thermotoga maritima} at 2.5 {\AA} resolution },
journal = { J. Mol. Biol. },
volume = { 246 },
pages = { 511 -- 521 }}
@article{TBJ_94_9999,
author = { A. Tomschy and G. B"ohm and R. Jaenicke },
title = { Ef\/fect of central and peripheral ion-pairs on the
thermal stability of D-glyceraldehyde-3- phosphate
dehydrogenase. },
year = 1994,
journal = { Eur. J. Biochem.},
volume = {??? },
pages = { ??? }}
@article{J_91_715 ,
author = { R. Jaenicke },
title = { Protein stability and molecular adaptation to extreme
conditions.},
year = 1991,
journal = { Eur J. Biochem.},
volume = { 202 },
pages = { 715--728 }}
@article{AGSW_87_34,
author = { L. Achenbach-{R}ichter and R. Gupta and K.O. Stetter
and C.R. Woese },
year = 1987,
journal = { System. Appl. Microbiol. },
volume = 9,
pages = { 34 -- 39 } }
@article{ARGZ_79_5698 ,
author = { P. Argos and M.G. Rossmann and U.M. Grau and H. Zuber
and G. Frank and J. Tratschin },
title = { Thermal stability and protein structure.},
year = 1979,
journal = { Biochemistry },
volume = { 18 },
pages = { 5698--5703 }}
@article{MA_89_397 ,
author = { L. Menendez-Arias and P. Argos },
title = { Engineering protein thermal stability. {S}equence
statistics point to residue substitutions in
$\alpha$-helices.},
year = 1989,
journal = { J. Mol. Biol.},
volume = { 206 },
pages = { 397--406 }}
@book{B_78_1,
author = { T.D. Brock },
title = { Thermophilic Microorganisms and Life at High Temperatures },
publisher = { Springer-Verlag},
year = 1978,
address = { New York, Heidelberg, Berlin },
pages = { 1 -- 11 } }
@incollection{TB_78_159,
author = { Tansey, M.R. and Brock, T.D. },
year = 1978,
type = { },
title = { Microbial life at high temperatures :
{E}cological aspects },
booktitle = { Microbial life in extreme environments },
editor = { Kushner, D.J. },
publisher = { Academic Press },
adress = { London, New York, San Francisco },
pages = { 159 -- 216 } }
@article{BZR_90_411,
author = { S. Brunie and C. Zelwer and J.-L. Riesler },
title = { Crystallographic studies at 2.5 {\AA} resolution of the
interaction of methionyl-t{RNA} synthetase from
\textit{E.coli}. },
year = 1990,
journal = { J. Mol. Biol.},
volume = { 216 },
pages = { 411--424 }}
@article{DSBW_91_221,
author = { S. Dao-pin and E. S"oderlind and W.A. Baase
and J.A. Wozniak and U. Sauer and B.W. Matthews },
year = 1991,
title = { Cumulated site directed charge change replacements
in bacteriophage {T}4 lysozyme suggest that long-range
electrostatic interactions contribute little to protein
stability. },
journal = { J. Mol. Biol. },
volume = 221,
pages = { 873 -- 887 } }
@article{DGLW_93_283 ,
author = { G.J. Davies and S.J. Gamblin and J.A. Littlechild and
H.C. Watson },
title = { The structure of a thermally stable 3-phosphoglycerate
kinase and a comparison with its mesophilic equivalent.},
year = 1993,
journal = { Proteins },
volume = { 15 },
pages = { 283--289 }}
@article{GP_90_9395 ,
author = { C. Ganther and A. Pl"uckthun },
title = { Gly to {A}la substitutions in helices of {GAPDH} :
ef\/fects on stability.},
year = 1990,
journal = { Biochemistry},
volume = { 29 },
pages = { 9395--9402 }}
@article{WWH_80_581 ,
author = { J.E. Walker and A.J. Wonacott and J.I. Harris },
title = { Heat stability of a tetrameric enzyme,
{d}-glyceraldehyde-3-phosphate dehydrogenase.},
year = 1980,
journal = { Eur. J. Biochem.},
volume = { 108 },
pages = { 581--586 }}
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MPI fuer Biochemie +49-89-8578-2685 (mol. biol. lab.)
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( korndoerfer at vms.biochem.mpg.de )
http://www.biochem.mpg.de:70/research-groups/xray/usr/korndoer/ingo.html
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Joel Sussman has just published a paper on the structure of a thermostable
enzyme and he addresses the issue there (Science or Nature, this year)
-that would be a start
Joe Mack
mack at ncifcrf.gov
I hope this helps.
Ronald
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