Diversity and subcellular distribution of archaeal secreted proteins

Z. Szabó, Mechthild Pohlschroder

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Secreted proteins make up a significant percentage of a prokaryotic proteome and play critical roles in important cellular processes such as polymer degradation, nutrient uptake, signal transduction, cell wall biosynthesis, and motility.The majority of archaeal proteins are believed to be secreted either in an unfolded conformation via the universally conserved Sec pathway or in a folded conformation via theTwin arginine transport (Tat) pathway. Extensive in vivo and in silico analyses of N-terminal signal peptides that target proteins to these pathways have led to the development of computational tools that not only predict Sec and Tat substrates with high accuracy but also provide information about signal peptide processing and targeting. Predictions therefore include indications as to whether a substrate is a soluble secreted protein, a membrane or cell wall anchored protein, or a surface structure subunit, and whether it is targeted for post-translational modification such as glycosylation or the addition of a lipid. The use of these in silico tools, in combination with biochemical and genetic analyses of transport pathways and their substrates, has resulted in improved predictions of the subcellular localization of archaeal secreted proteins, allowing for a more accurate annotation of archaeal proteomes, and has led to the identification of potential adaptations to extreme environments, as well as phyla-specific pathways among the archaea. A more comprehensive understanding of the transport pathways used and post-translational modifications of secreted archaeal proteins will also facilitate the identification and heterologous expression of commercially valuable archaeal enzymes.

Original languageEnglish
JournalFrontiers in Microbiology
Volume3
Issue numberJUL
DOIs
Publication statusPublished - 2012

Fingerprint

Archaeal Proteins
Proteome
Post Translational Protein Processing
Protein Sorting Signals
Computer Simulation
Cell Wall
Arginine
Proteins
Archaea
Glycosylation
Cell Movement
Molecular Biology
Signal Transduction
Polymers
Membrane Proteins
Lipids
Enzymes

Keywords

  • Archaea
  • Archaeosortase
  • Cell surface structures
  • Lipoprotein
  • Pili
  • Protein transport
  • Sec transport
  • Tat transport

ASJC Scopus subject areas

  • Microbiology
  • Microbiology (medical)

Cite this

Diversity and subcellular distribution of archaeal secreted proteins. / Szabó, Z.; Pohlschroder, Mechthild.

In: Frontiers in Microbiology, Vol. 3, No. JUL, 2012.

Research output: Contribution to journalArticle

@article{2818e44ae3b64766b632eb8dd33df3cc,
title = "Diversity and subcellular distribution of archaeal secreted proteins",
abstract = "Secreted proteins make up a significant percentage of a prokaryotic proteome and play critical roles in important cellular processes such as polymer degradation, nutrient uptake, signal transduction, cell wall biosynthesis, and motility.The majority of archaeal proteins are believed to be secreted either in an unfolded conformation via the universally conserved Sec pathway or in a folded conformation via theTwin arginine transport (Tat) pathway. Extensive in vivo and in silico analyses of N-terminal signal peptides that target proteins to these pathways have led to the development of computational tools that not only predict Sec and Tat substrates with high accuracy but also provide information about signal peptide processing and targeting. Predictions therefore include indications as to whether a substrate is a soluble secreted protein, a membrane or cell wall anchored protein, or a surface structure subunit, and whether it is targeted for post-translational modification such as glycosylation or the addition of a lipid. The use of these in silico tools, in combination with biochemical and genetic analyses of transport pathways and their substrates, has resulted in improved predictions of the subcellular localization of archaeal secreted proteins, allowing for a more accurate annotation of archaeal proteomes, and has led to the identification of potential adaptations to extreme environments, as well as phyla-specific pathways among the archaea. A more comprehensive understanding of the transport pathways used and post-translational modifications of secreted archaeal proteins will also facilitate the identification and heterologous expression of commercially valuable archaeal enzymes.",
keywords = "Archaea, Archaeosortase, Cell surface structures, Lipoprotein, Pili, Protein transport, Sec transport, Tat transport",
author = "Z. Szab{\'o} and Mechthild Pohlschroder",
year = "2012",
doi = "10.3389/fmicb.2012.00207",
language = "English",
volume = "3",
journal = "Frontiers in Microbiology",
issn = "1664-302X",
publisher = "Frontiers Media S. A.",
number = "JUL",

}

TY - JOUR

T1 - Diversity and subcellular distribution of archaeal secreted proteins

AU - Szabó, Z.

AU - Pohlschroder, Mechthild

PY - 2012

Y1 - 2012

N2 - Secreted proteins make up a significant percentage of a prokaryotic proteome and play critical roles in important cellular processes such as polymer degradation, nutrient uptake, signal transduction, cell wall biosynthesis, and motility.The majority of archaeal proteins are believed to be secreted either in an unfolded conformation via the universally conserved Sec pathway or in a folded conformation via theTwin arginine transport (Tat) pathway. Extensive in vivo and in silico analyses of N-terminal signal peptides that target proteins to these pathways have led to the development of computational tools that not only predict Sec and Tat substrates with high accuracy but also provide information about signal peptide processing and targeting. Predictions therefore include indications as to whether a substrate is a soluble secreted protein, a membrane or cell wall anchored protein, or a surface structure subunit, and whether it is targeted for post-translational modification such as glycosylation or the addition of a lipid. The use of these in silico tools, in combination with biochemical and genetic analyses of transport pathways and their substrates, has resulted in improved predictions of the subcellular localization of archaeal secreted proteins, allowing for a more accurate annotation of archaeal proteomes, and has led to the identification of potential adaptations to extreme environments, as well as phyla-specific pathways among the archaea. A more comprehensive understanding of the transport pathways used and post-translational modifications of secreted archaeal proteins will also facilitate the identification and heterologous expression of commercially valuable archaeal enzymes.

AB - Secreted proteins make up a significant percentage of a prokaryotic proteome and play critical roles in important cellular processes such as polymer degradation, nutrient uptake, signal transduction, cell wall biosynthesis, and motility.The majority of archaeal proteins are believed to be secreted either in an unfolded conformation via the universally conserved Sec pathway or in a folded conformation via theTwin arginine transport (Tat) pathway. Extensive in vivo and in silico analyses of N-terminal signal peptides that target proteins to these pathways have led to the development of computational tools that not only predict Sec and Tat substrates with high accuracy but also provide information about signal peptide processing and targeting. Predictions therefore include indications as to whether a substrate is a soluble secreted protein, a membrane or cell wall anchored protein, or a surface structure subunit, and whether it is targeted for post-translational modification such as glycosylation or the addition of a lipid. The use of these in silico tools, in combination with biochemical and genetic analyses of transport pathways and their substrates, has resulted in improved predictions of the subcellular localization of archaeal secreted proteins, allowing for a more accurate annotation of archaeal proteomes, and has led to the identification of potential adaptations to extreme environments, as well as phyla-specific pathways among the archaea. A more comprehensive understanding of the transport pathways used and post-translational modifications of secreted archaeal proteins will also facilitate the identification and heterologous expression of commercially valuable archaeal enzymes.

KW - Archaea

KW - Archaeosortase

KW - Cell surface structures

KW - Lipoprotein

KW - Pili

KW - Protein transport

KW - Sec transport

KW - Tat transport

UR - http://www.scopus.com/inward/record.url?scp=84875766625&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84875766625&partnerID=8YFLogxK

U2 - 10.3389/fmicb.2012.00207

DO - 10.3389/fmicb.2012.00207

M3 - Article

C2 - 22783239

AN - SCOPUS:84875766625

VL - 3

JO - Frontiers in Microbiology

JF - Frontiers in Microbiology

SN - 1664-302X

IS - JUL

ER -