Signal peptides of secreted proteins of the archaeon Sulfolobus solfataricus : a genomic survey

Abstract

Signal peptides of secreted proteins of the archaeon Sulfolobus solfataricus: a genomic survey Albers, S.V.; Driessen, A.J.M. Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim.Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. Download date: 23-03-2019Abstract Analysis of the recently completed genome sequence of the thermoacidophilic archaeon Sulfolobus solfataricus reveals that about 4.2% of its proteome consists of putative secretory proteins with signal peptides. This includes members of the four major classes of signal peptides: secretory signal peptides, twin-arginine signal peptides, possible lipoprotein precursors, and type IV pilin signal peptides. The latter group is surprisingly large compared to the size of the groups in other organisms and seems to be used predominately for a subset of extracellular substrate-binding proteins.

Targeted Disruption of the α-Amylase Gene in the Hyperthermophilic Archaeon Sulfolobus solfataricus

“…Comparison between the N-terminal region of SSO1172 and that of other membrane-associated or secreted S. solfataricus proteins (1,9) suggested that this region encoded a signal peptide. Comparison with other functionally related hyperthermophilic archaeal enzymes revealed conservation of a C-terminal hydrophobic region (10).…”

Insights into ABC Transport in Archaea

“…In Pyrobaculum aerophilum the region after the hydrophobic stretch is enriched in glutamine residues, which have been shown in S. solfataricus to be at the +1 site of the cleavage site of two binding protein of the di/oligopeptide class ( Fig. 2; Albers and Driessen, 2002;Elferink et al, 2001). One of the signal peptides of S. tokodaii appears similar to the one found in M. kandlerii, whereas all signal peptides of binding proteins from the sugar class of S. solfataricus are homologous to type IV prepilin signal peptides (Albers et al, 1999a,b;Elferink et al, 2001).…”

“…2), although it is difficult to predict a consensus sequence for the type I signal peptidase. Four extracellular proteins, the S-layer protein and three substrate-binding proteins were N-terminally sequenced (Albers and Driessen, 2002;Elferink et al, 2001). Two of the resulting signal peptide cleavage sites are shown in Fig.…”

Protein transport in the halophilic archaeon Halobacterium sp. NRC-1: a major role for the twin-arginine translocation pathway?

“…This represents 1 % of the proteome, which is relatively low as compared with for instance Bacillus subtilis (4 % ; Tjalsma et al, 2000), E. coli (6 % ; unpublished results) or S. solfataricus (4%; Albers & Driessen, 2002). The N-regions of these signal peptides usually contain one or two positively charged residues, with a strong bias to arginines (18 % Lys, 82 % Arg).…”

“…Through genomic analysis, the eurarchaeon Methanococcus jannaschii was predicted to contain at least 34 secretory proteins , but the criteria used for identification of proteins containing signal peptides were rather conservative and it is likely that several were not identified. Recently, a more extensive survey was performed on the genome of Sulfolobus solfataricus, a member of the crenarchaeotes (Albers & Driessen, 2002). In that case, Protein transport in Halobacterium sp.…”