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Small Stress Response Proteins in Escherichia coli: Proteins Missed by Classical Proteomic Studies

Proteins of 50 or fewer amino acids are poorly characterized in all organisms. The corresponding genes are challenging to reliably annotate, and it is difficult to purify and characterize the small protein products. Due to these technical limitations, little is known about the abundance of small pro... Full description

Journal Title: The Journal of Bacteriology 2010, Vol. 192(1), p.46
Main Author: Hemm, Matthew R.
Other Authors: Paul, Brian J. , Miranda-Rios, Juan , Zhang, Aixia , Soltanzad, Nima , Storz, Gisela
Format: Electronic Article Electronic Article
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ID: ISSN: 0021-9193 ; PMID: 19734316
Link: http://jb.asm.org/cgi/content/abstract/192/1/46
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recordid: asm19734316
title: Small Stress Response Proteins in Escherichia coli: Proteins Missed by Classical Proteomic Studies
format: Article
creator:
  • Hemm, Matthew R.
  • Paul, Brian J.
  • Miranda-Rios, Juan
  • Zhang, Aixia
  • Soltanzad, Nima
  • Storz, Gisela
subjects:
  • Escherichia Coli -- Physiological Aspects
  • Bacterial Proteins -- Properties
ispartof: The Journal of Bacteriology, 2010, Vol. 192(1), p.46
description: Proteins of 50 or fewer amino acids are poorly characterized in all organisms. The corresponding genes are challenging to reliably annotate, and it is difficult to purify and characterize the small protein products. Due to these technical limitations, little is known about the abundance of small proteins, not to mention their biological functions. To begin to characterize these small proteins in Escherichia coli, we assayed their accumulation under a variety of growth conditions and after exposure to stress. We found that many small proteins accumulate under specific growth conditions or are stress induced. For some genes, the observed changes in protein levels were consistent with known transcriptional regulation, such as ArcA activation of the operons encoding yccB and ybgT. However, we also identified novel regulation, such as Zur repression of ykgMO, cyclic AMP response protein (CRP) repression of azuC, and CRP activation of ykgR. The levels of 11 small proteins increase after heat shock, and induction of at least I of these, YobF, occurs at a posttranscriptional level. These results show that small proteins are an overlooked subset of stress response proteins in E. coli and provide information that will be valuable for determining the functions of these proteins. doi: 10.1128/JB.00872-09
language:
source:
identifier: ISSN: 0021-9193 ; PMID: 19734316
fulltext: fulltext
issn:
  • 0021-9193
  • 00219193
url: Link


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titleSmall Stress Response Proteins in Escherichia coli: Proteins Missed by Classical Proteomic Studies
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descriptionProteins of 50 or fewer amino acids are poorly characterized in all organisms. The corresponding genes are challenging to reliably annotate, and it is difficult to purify and characterize the small protein products. Due to these technical limitations, little is known about the abundance of small proteins, not to mention their biological functions. To begin to characterize these small proteins in Escherichia coli, we assayed their accumulation under a variety of growth conditions and after exposure to stress. We found that many small proteins accumulate under specific growth conditions or are stress induced. For some genes, the observed changes in protein levels were consistent with known transcriptional regulation, such as ArcA activation of the operons encoding yccB and ybgT. However, we also identified novel regulation, such as Zur repression of ykgMO, cyclic AMP response protein (CRP) repression of azuC, and CRP activation of ykgR. The levels of 11 small proteins increase after heat shock, and induction of at least I of these, YobF, occurs at a posttranscriptional level. These results show that small proteins are an overlooked subset of stress response proteins in E. coli and provide information that will be valuable for determining the functions of these proteins. doi: 10.1128/JB.00872-09
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