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The sequence of a subtilisin-type protease (aerolysin) from the hyperthermophilic archaeum Pyrobaculum aerophilum reveals sites important to thermostability by Paul Völkl; Peter Markiewicz; Karl O. Stetter; Jeffrey H. Miller is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract The hyperthermophilic archaeum __Pyrobaculum aerophilum__ grows optimally at 100 °C and pH 7.0. Cell homogenates exhibit strong proteolytic activity within a temperature range of 80–130 °C. During an analysis of cDNA and genomic sequence tags, a genomic clone was recovered showing strong sequence homology to alkaline subtilisins of __Bacillus__ sp. The total DNA sequence of the gene encoding the protease (named “aerolysin”) was determined. Multiple sequence alignment with 15 different serine‐type proteases showed greatest homology with subtilisins from gram‐positive bacteria rather than archaeal or eukaryal serine proteases. Models of secondary and tertiary structure based on sequence alignments and the tertiary structures of subtilisin Carlsberg, BPN', thermitase, and protease K were generated for __P. aerophilum__ subtilisin. This allowed identification of sites potentially contributing to the thermostability of the protein. One common transition put alanines at the beginning and end of surface alpha‐helices. Aspartic acids were found at the N‐terminus of several surface helices, possibly increasing stability by interacting with the helix dipole. Several of the substi

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Author

Paul Völkl; Peter Markiewicz; Karl O. Stetter; Jeffrey H. Miller

Publisher

Cold Spring Harbor Laboratory Press; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley (ISSN 0961-8368)

Published

1994

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)