Dissection of key determinants of cleavage activity in signal peptidase III (SPaseIII) PibD
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- 作者：Anna-Lena Henche (1)
Marleen van Wolferen (1)
Abhrajyoti Ghosh (2)
Sonja-Verena Albers (1) - 关键词：Aspartate protease ; Archaea ; Type IV pilus ; In vivo cleavage assay
- 刊名：Extremophiles
- 出版年：2014
- 出版时间：September 2014
- 年：2014
- 卷：18
- 期：5
- 页码：905-913
- 全文大小：999 KB
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Marleen van Wolferen (1)
Abhrajyoti Ghosh (2)
Sonja-Verena Albers (1)
1. Molecular Biology of Archaea, Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch Strasse 10, 35043, Marburg, Germany
2. Department of Biochemistry, Bose Institute, Centenary Campus, P 1/12 C.I.T Road, Scheme-VIIM, Kolkata, 700054, West Bengal, India - ISSN：1433-4909
文摘
In Archaea, type IV prepilins and prearchaellins are processed by designated signal peptidase III (SPaseIII) prior to their incorporation into pili and the archaellum, respectively. These peptidases belong to the family of integral membrane aspartic acid proteases that contain two essential aspartate residues of which the second aspartate is located in a conserved GxGD motif. To this group also bacterial type IV prepilin peptidases, Alzheimer disease-related secretases, signal peptide peptidases and signal peptide peptidase-like proteases in humans belong. Here we have performed detailed in vivo analyses to understand the cleavage activity of PibD, SPaseIII from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. Using an already established in vivo heterologous system cleavage assay, we could successfully identify the key amino acid residues essential for catalysis of PibD. Furthermore, in trans complementation of a pibD S. acidocaldarius deletion mutant with PibD variants having substituted key amino acids has consolidated our observations of the importance of these residues in catalysis. Based on our data, we propose to re-define class III peptidases/type IV prepilin/prearchaellin peptidases as GxHyD group (rather than GxGD) of proteases [Hy-hydrophobic amino acid].