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Bacterial metal detectors
Author(s) -
Buchanan Susan K.
Publication year - 2005
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2005.04904.x
Subject(s) - periplasmic space , biology , sigma factor , bacterial outer membrane , inner membrane , riboswitch , microbiology and biotechnology , signal transduction , transcription factor , membrane transport protein , transcription (linguistics) , biochemistry , transporter , computational biology , gene , rna polymerase , membrane , rna , escherichia coli , non coding rna , linguistics , philosophy
Summary Gram negative bacteria can detect environmental iron using outer membrane transporters (OMTs), and then regulate certain transport genes to take advantage of a readily available iron source. This process begins with an iron complex being bound by an OMT, and results in a signal being sent across the outer membrane, the periplasmic space, and the inner membrane, to a sigma factor that interacts with RNA polymerase and initiates transcription of relevant genes. Many of the interactions contributing to signalling have been observed by genetic and biochemical studies, but structural studies, which potentially show these interactions in molecular detail, have been limited. In this issue, Garcia‐Herrero and Vogel describe an NMR structure of the periplasmic domain of an OMT, which had not been seen in previous X‐ray crystal structures. This domain transmits the ‘iron availability’ signal to the next protein in the signal transduction cascade, which sits in the inner membrane and extends into the periplasm. The new structure extends our knowledge of transporter architecture and suggests how signalling may occur across the outer membrane.