Proteomic and computational analysis of secreted proteins with type 1 signal peptides from the antarctic archaeon Methanococcoides burtonii
LC-MS/MS was used to identify secreted proteins in the Antarctic archaeon Methanococcoides burtonii. Seven proteins possessing a classical class 1 signal peptide were identified in the supernatant from cultures grown at 4 and 23 C. The proteins included a putative S-layer cell surface protein, cell...
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2006
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ftunivqespace:oai:espace.library.uq.edu.au:UQ:113450 2023-05-15T13:31:21+02:00 Proteomic and computational analysis of secreted proteins with type 1 signal peptides from the antarctic archaeon Methanococcoides burtonii Saunders, N. F. W. Ng, C. Raftery, M. Guilhaus, M. Goodchild, A. Cavicchioli, R. 2006-01-01 https://espace.library.uq.edu.au/view/UQ:113450 eng eng Amer Chemical Soc doi:10.1021/pr060220x issn:1535-3893 Biochemical Research Methods LC-MS/MS secretion supernatant fraction type 1 signal peptides archaea cold adaptation psychrophile protease S-layer protein SignaIP Methanosarcina-mazei Polyacrylamide Gels Translocation Membrane Domains Disaggregatase Prediction Evolution Sequence Journal Article 2006 ftunivqespace https://doi.org/10.1021/pr060220x 2020-08-04T06:37:34Z LC-MS/MS was used to identify secreted proteins in the Antarctic archaeon Methanococcoides burtonii. Seven proteins possessing a classical class 1 signal peptide were identified in the supernatant from cultures grown at 4 and 23 C. The proteins included a putative S-layer cell surface protein, cell surface protein involved with cell adhesion, and trypsin-like serine protease. Protease activity was detected in the secreted fraction, and the signal peptide cleavage site of the protease was confirmed using Edman sequencing. The expression profile of putative cell surface proteins suggests a requirement for cell interactions during growth at low temperature. Sequences of the secreted proteins were used to compile a dataset containing a further 32 predicted secreted proteins from the Methanosarcinaceae. Many of these proteins were also S-layer cell surface proteins with a variety of predicted roles, particularly in cell-cell interaction. Computational analysis of signal peptides revealed a preference for lysine in the n-region, leucine in the h-region, and a eucaryal-type cleavage site, highlighting the mosaic nature of signal peptides in Archaea. This is the first study to experimentally characterize secreted proteins from a cold-adapted archaeon and provides new insight and a functional dataset for studying secretion in Archaea. Article in Journal/Newspaper Antarc* Antarctic The University of Queensland: UQ eSpace Antarctic The Antarctic Journal of Proteome Research 5 9 2457 2464 |
institution |
Open Polar |
collection |
The University of Queensland: UQ eSpace |
op_collection_id |
ftunivqespace |
language |
English |
topic |
Biochemical Research Methods LC-MS/MS secretion supernatant fraction type 1 signal peptides archaea cold adaptation psychrophile protease S-layer protein SignaIP Methanosarcina-mazei Polyacrylamide Gels Translocation Membrane Domains Disaggregatase Prediction Evolution Sequence |
spellingShingle |
Biochemical Research Methods LC-MS/MS secretion supernatant fraction type 1 signal peptides archaea cold adaptation psychrophile protease S-layer protein SignaIP Methanosarcina-mazei Polyacrylamide Gels Translocation Membrane Domains Disaggregatase Prediction Evolution Sequence Saunders, N. F. W. Ng, C. Raftery, M. Guilhaus, M. Goodchild, A. Cavicchioli, R. Proteomic and computational analysis of secreted proteins with type 1 signal peptides from the antarctic archaeon Methanococcoides burtonii |
topic_facet |
Biochemical Research Methods LC-MS/MS secretion supernatant fraction type 1 signal peptides archaea cold adaptation psychrophile protease S-layer protein SignaIP Methanosarcina-mazei Polyacrylamide Gels Translocation Membrane Domains Disaggregatase Prediction Evolution Sequence |
description |
LC-MS/MS was used to identify secreted proteins in the Antarctic archaeon Methanococcoides burtonii. Seven proteins possessing a classical class 1 signal peptide were identified in the supernatant from cultures grown at 4 and 23 C. The proteins included a putative S-layer cell surface protein, cell surface protein involved with cell adhesion, and trypsin-like serine protease. Protease activity was detected in the secreted fraction, and the signal peptide cleavage site of the protease was confirmed using Edman sequencing. The expression profile of putative cell surface proteins suggests a requirement for cell interactions during growth at low temperature. Sequences of the secreted proteins were used to compile a dataset containing a further 32 predicted secreted proteins from the Methanosarcinaceae. Many of these proteins were also S-layer cell surface proteins with a variety of predicted roles, particularly in cell-cell interaction. Computational analysis of signal peptides revealed a preference for lysine in the n-region, leucine in the h-region, and a eucaryal-type cleavage site, highlighting the mosaic nature of signal peptides in Archaea. This is the first study to experimentally characterize secreted proteins from a cold-adapted archaeon and provides new insight and a functional dataset for studying secretion in Archaea. |
format |
Article in Journal/Newspaper |
author |
Saunders, N. F. W. Ng, C. Raftery, M. Guilhaus, M. Goodchild, A. Cavicchioli, R. |
author_facet |
Saunders, N. F. W. Ng, C. Raftery, M. Guilhaus, M. Goodchild, A. Cavicchioli, R. |
author_sort |
Saunders, N. F. W. |
title |
Proteomic and computational analysis of secreted proteins with type 1 signal peptides from the antarctic archaeon Methanococcoides burtonii |
title_short |
Proteomic and computational analysis of secreted proteins with type 1 signal peptides from the antarctic archaeon Methanococcoides burtonii |
title_full |
Proteomic and computational analysis of secreted proteins with type 1 signal peptides from the antarctic archaeon Methanococcoides burtonii |
title_fullStr |
Proteomic and computational analysis of secreted proteins with type 1 signal peptides from the antarctic archaeon Methanococcoides burtonii |
title_full_unstemmed |
Proteomic and computational analysis of secreted proteins with type 1 signal peptides from the antarctic archaeon Methanococcoides burtonii |
title_sort |
proteomic and computational analysis of secreted proteins with type 1 signal peptides from the antarctic archaeon methanococcoides burtonii |
publisher |
Amer Chemical Soc |
publishDate |
2006 |
url |
https://espace.library.uq.edu.au/view/UQ:113450 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
doi:10.1021/pr060220x issn:1535-3893 |
op_doi |
https://doi.org/10.1021/pr060220x |
container_title |
Journal of Proteome Research |
container_volume |
5 |
container_issue |
9 |
container_start_page |
2457 |
op_container_end_page |
2464 |
_version_ |
1766017651321077760 |