1994•Unpublished venueRequires access
Pressure Stabilization ofProteins fromExtreme Thermophiles
Derek J. HEItANDDOUGLAS, Suzanne Clark
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Abstract
We describe thestabilization bypressure ofenzymes, including a hydrogenase fromMethanococcus jannaschii, anextremely thermophilic deep-sea methanogen. Thisisthefirst published report ofproteins from thermophiles beingstabilized bypressure. Inactivation studies ofpartially purified hydrogenases froman extreme thermophile (Methanococcus igneus), amoderate thermophile (Methanococcus thermolithotrophicus), andamesophile (Methanococcus maripaludis), allfromshallow marinesites, showthatpressure stabilization isnotunique toenzymes isolated fromhigh-pressure environments. Thesestudies suggest thatpressure stabilization ofanenzyme mayberelated toitsthermophilicity. Further experiments comparing theeffects of increased pressure onthestability offt-glucosidases fromthehyperthermophile Pyrococcus furiosus and Saccharomyces cerevisiae support thispossibility. We havealsoexamined pressure effects onseveral highly homologous glyceraldehyde-3-phosphate dehydrogenases frommesophilic andthermophilic sources anda rubredoxin fromP.furiosus. Theresults suggest thathydrophobic interactions, whichhavebeenimplicated in thestabilization ofmanythermophilic proteins, contribute tothepressure stabilization ofenzymes from thermophiles.