Back to Search Start Over

Prevalent association with the bacterial cell envelope of prokaryotic expansins revealed by bioinformatics analysis.

Authors :
de Sandozequi, Andrés
Salazar‐Cortés, Juan José
Tapia‐Vázquez, Irán
Martínez‐Anaya, Claudia
Source :
Protein Science: A Publication of the Protein Society; May2022, Vol. 31 Issue 5, p1-14, 14p
Publication Year :
2022

Abstract

Expansins are a group of proteins from diverse organisms from bacteria to plants. Although expansins show structural conservation, their biological roles seem to differ among kingdoms. In plants, these proteins remodel the cell wall during plant growth and other processes. Contrarily, determination of bacterial expansin activity has proven difficult, although genetic evidence of bacterial mutants indicates that expansins participate in bacteria–plant interactions. Nevertheless, a large proportion of expansin genes are found in the genomes of free‐living bacteria, suggesting roles that are independent of the interaction with living plants. Here, we analyzed all available sequences of prokaryotic expansins for correlations between surface electric charge, extra protein modules, and sequence motifs for association with the bacteria exterior after export. Additionally, information on the fate of protein after translocation across the membrane also points to bacterial cell association of expansins through six different mechanisms, such as attachment of a lipid molecule for membrane anchoring in diderm species or covalent linking to the peptidoglycan layer in monoderms such as the Bacilliales. Our results have implications for expansin function in the context of bacteria–plant interactions and also for free‐living species in which expansins might affect cell–cell or cell–substrate interaction properties and indicate the need to re‐examine the roles currently considered for these proteins. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
09618368
Volume :
31
Issue :
5
Database :
Complementary Index
Journal :
Protein Science: A Publication of the Protein Society
Publication Type :
Academic Journal
Accession number :
156583981
Full Text :
https://doi.org/10.1002/pro.4315