Abstract
ABSTRACTIn the 1960s several groups reported the isolation and preliminary genetic mapping of Escherichia coli strains tolerant towards the action of colicins. These pioneering studies kick-started two new fields in bacteriology; one centred on how bacteriocins like colicins exploit the Tol (or more commonly Tol-Pal) system to kill bacteria, the other on the physiological role of this cell envelope-spanning assembly. The following half century has seen significant advances in the first of these fields whereas the second has remained elusive, until recently. Here, we review work that begins to shed light on Tol-Pal function in Gram-negative bacteria. What emerges from these studies is that Tol-Pal is an energised system with fundamental, interlinked roles in cell division – coordinating the re-structuring of peptidoglycan at division sites and stabilising the connection between the outer membrane and underlying cell wall. This latter role is achieved by Tol-Pal exploiting the proton motive force to catalyse the accumulation of the outer membrane peptidoglycan associated lipoprotein Pal at division sites while simultaneously mobilising Pal molecules from around the cell. These studies begin to explain the diverse phenotypic outcomes of tol-pal mutations, point to other cell envelope roles Tol-Pal may have and raise many new questions.
Highlights
INTRODUCTION & BACKGROUNDThe cell envelope of Gram-negative bacteria is comprised of a symmetric inner membrane and an asymmetric outer membrane with an intervening layer of peptidoglycan (PG) in the periplasm
We review work that begins to shed light on Tol-Pal function in Gram-negative bacteria. What emerges from these studies is that Tol-Pal is an energised system with fundamental, interlinked roles in cell division – coordinating the re-structuring of peptidoglycan at division sites and stabilising the connection between the outer membrane and underlying cell wall
This latter role is achieved by Tol-Pal exploiting the proton motive force to catalyse the accumulation of the outer membrane peptidoglycan associated lipoprotein Pal at division sites while simultaneously mobilising Pal molecules from around the cell
Summary
INTRODUCTION & BACKGROUNDThe cell envelope of Gram-negative bacteria is comprised of a symmetric inner membrane and an asymmetric outer membrane with an intervening layer of peptidoglycan (PG) in the periplasm. The following sections summarise what is known of the structure and the function of core components of the Tol-Pal system; TolQ, TolR, TolA in the inner membrane, TolB in the periplasm and Pal in the outer membrane.
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