Suppression of the Temperature-Sensitive Mutation of thebamDGene Required for the Assembly of Outer Membrane Proteins by Multicopy of theyiaDGene inEscherichia coli

2011 ◽  
Vol 75 (1) ◽  
pp. 162-164 ◽  
Author(s):  
Tomoaki TACHIKAWA ◽  
Jun-ichi KATO
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Temperature Sensitive ◽  
Inescherichia Coli ◽  
Temperature Sensitive Mutation

scholarly journals Phase-variable outer membrane proteins inEscherichia coli

1996 ◽  
Vol 16 (2) ◽  
pp. 63-76 ◽  
Author(s):  
Peter Owen ◽  
Mary Meehan ◽  
Helen de Loughry-Doherty ◽  
Ian Henderson
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Phase Variable ◽  
Inescherichia Coli

Identification and Network of Outer Membrane Proteins Regulating Streptomysin Resistance inEscherichia coli

2008 ◽  
Vol 7 (9) ◽  
pp. 4040-4049 ◽  
Author(s):  
Hui Li ◽  
Bao-Cheng Wang ◽  
Wen-Jiao Xu ◽  
Xiang-Min Lin ◽  
Xuan-Xian Peng
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Inescherichia Coli

scholarly journals The Conservation of Low Complexity Regions in Bacterial Proteins Depends on the Pathogenicity of the Strain and Subcellular Location of the Protein

Genes ◽  
2021 ◽  
Vol 12 (3) ◽  
pp. 451
Author(s):  
Pablo Mier ◽  
Miguel A. Andrade-Navarro
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Bacterial Species ◽  
Outer Membrane Proteins ◽  
Subcellular Location ◽  
Low Complexity ◽  
Extracellular Proteins ◽  
Bacterial Strains ◽  
Bacterial Proteins ◽  
Protein Subcellular Location

Low complexity regions (LCRs) in proteins are characterized by amino acid frequencies that differ from the average. These regions evolve faster and tend to be less conserved between homologs than globular domains. They are not common in bacteria, as compared to their prevalence in eukaryotes. Studying their conservation could help provide hypotheses about their function. To obtain the appropriate evolutionary focus for this rapidly evolving feature, here we study the conservation of LCRs in bacterial strains and compare their high variability to the closeness of the strains. For this, we selected 20 taxonomically diverse bacterial species and obtained the completely sequenced proteomes of two strains per species. We calculated all orthologous pairs for each of the 20 strain pairs. Per orthologous pair, we computed the conservation of two types of LCRs: compositionally biased regions (CBRs) and homorepeats (polyX). Our results show that, in bacteria, Q-rich CBRs are the most conserved, while A-rich CBRs and polyA are the most variable. LCRs have generally higher conservation when comparing pathogenic strains. However, this result depends on protein subcellular location: LCRs accumulate in extracellular and outer membrane proteins, with conservation increased in the extracellular proteins of pathogens, and decreased for polyX in the outer membrane proteins of pathogens. We conclude that these dependencies support the functional importance of LCRs in host–pathogen interactions.

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