Abstract: The present invention relates to maintaining the activity and stability of enzymes and biologically active proteins at increased temperatures by contacting same with a combination of isolated passive and active chaperones from a hyperthermopilic Archaeon, wherein the chaperones may include heat shock proteins, prefoldin and/or chaperonin proteins.

Abstract: The invention provides methods and compositions for increasing tolerance of microorganisms to toxic agents, such as solvents; and for increasing production of solvents from solvent-generating microorganisms. The methods comprise engineering a microorganism of interest to express a heterologous heat-shock protein/chaperone, e.g., Group II chaperonin or a prefoldin such as ?-prefoldin, where the heterologous protein is from an extremophile, such as an archaean.

Abstract: The present invention relates to recombinant protein production, and more specifically, to methods for recovery of properly folder bioactive proteins by expressing chaperone genes from extremophilic Archaea, during recombinant protein synthesis in a host cell thereby significantly improving recovery of properly folded bioactive proteins.

Abstract: The invention provides methods and compositions for increasing tolerance of microorganisms to toxic agents, such as solvents; and for increasing production of solvents from solvent-generating microorganisms. The methods comprise engineering a microorganism of interest to express a heterologous heat-shock protein/chaperone, e.g., Group II chaperonin or a prefoldin such as ?-prefoldin, where the heterologous protein is from an extremophile, such as an archaean.

Abstract: The present invention relates to maintaining the activity and stability of enzymes and biologically active proteins at increased temperatures by contacting same with a combination of isolated passive and active chaperones from a hyperthermopilic Archaeon, wherein the chaperones may include heat shock proteins, prefoldin and/or chaperonin proteins.

Abstract: Small heat shock proteins, e.g., Pyrococcus fuiosus (Pfu-sHSP and/or Pfu-tsHSP), confer thermotolerance on cellular cultures and on proteins in cellular extracts during prolonged incubation at elevated temperature, demonstrating the ability to protect cellular proteins and maintain cellular viability under heat stress conditions. Such heat shock proteins are effective to combat enzymatic aggregation and intracellular precipitation during heat stress, and thereby enable enhancement of the utility and stability of enzymes in various applications, e.g., Taq polymerase in PCR applications, digestive enzymes in microbial degradative applications, etc.

Abstract: Small heat shock proteins, e.g., Pyrococcus fuiosus (Pfu-sHSP and/or Pfu-tsHSP), confer thermotolerance on cellular cultures and on proteins in cellular extracts during prolonged incubation at elevated temperature, demonstrating the ability to protect cellular proteins and maintain cellular viability under heat stress conditions. Such heat shock proteins are effective to combat enzymatic aggregation and intracellular precipitation during heat stress, and thereby enable enhancement of the utility and stability of enzymes in various applications, e.g., Taq polymerase in PCR applications, digestive enzymes in microbial degradative applications, etc.

Abstract: Small heat shock proteins, e.g., Pyrococcus fuiosus (Pfu-sHSP), confer thermotolerance on cellular cultures and on proteins in cellular extracts during prolonged incubation at elevated temperature, demonstrating the ability to protect cellular proteins and maintain cellular viability under heat stress conditions. Such heat shock proteins are effective to combat enzymatic aggregation and intracellular precipitation during heat stress, and thereby enable enhancement of the utility and stability of enzymes in various applications, e.g., Taq polymerase in PCR applications, digestive enzymes in microbial degradative applications, etc.

Abstract: Small heat shock proteins, e.g., Pyrococcus fuiosus (Pfu-sHSP), confer thermotolerance on cellular cultures and on proteins in cellular extracts during prolonged incubation at elevated temperature, demonstrating the ability to protect cellular proteins and maintain cellular viability under heat stress conditions. Such heat shock proteins are effective to combat enzymatic aggregation and intracellular precipitation during heat stress, and thereby enable enhancement of the utility and stability of enzymes in various applications, e.g., Taq polymerase in PCR applications, digestive enzymes in microbial degradative applications, etc.

Abstract: Purified nucleic acid comprising a nucleotide base sequence selected from sequence ID NOS.: 1-9.

Abstract: Purified nucleic acid comprising a nucleotide base sequence selected from sequence ID NOS.: 1-8.