cotranslational protein targeting to the plasma membrane, the Ffh-4.5S RNA ribonucleoprotein complex and the FtsY protein, respectively, form a unique complex in which both Ffh and FtsY act as GTPase activating proteins for one another, resulting in a mutual stimulation of GTP hydrolysis by both proteins, 4.5S RNA modulates the conformation of the Ffh-FtsY complex and may regulate its GTPase activity during the SRP functional cycle
Ffh mediates SRP-dependent, cotranslational protein targeting to the plasma membrane, Ffh and FtsY, the latter being the GTPase subunit of the bacterial SRP receptor, act as GTPase activating proteins for one another, resulting in reciprocal stimulation of GTP hydrolysis
protein targeting by the SRP pathway, Ffh and FtsY, the GTPase subunit of the SRP receptor, reciprocally regulate each others GTPase activity, they interact only in a primed conformation which requires interdomain communication
protein targeting by the SRP pathway, Ffh and FtsY, the GTPase subunit of the SRP receptor, reciprocally regulate each others GTPase activity, they interact only in a primed conformation which requires interdomain communication
protein targeting to the plasma membrane, signal recognition particle cycle, SRP and its receptor stimulate each others GTPase activity, GTP hydrolysis ensures unidirectional targeting of cargo through a translocation pore in the membrane
the signal recognition particle mediates the co-translational targeting of nascent proteins to the bacterial plasma membrane. During this process, two GTPases, one in the signal recognition particle and one in the signal recogition particle receptor, form a complex in which both proteins reciprocally activate the GTPase reaction of one another. Crystal structures of the complex of signal recognition particle and signal recogition particle receptor show that the two GTPases associate via an unusually extensive and highly cooperative interaction surface and form a composite active site at the interface. GTPase activation proceeds through a unique mechanism, stimulated by both interactions between the twinned GTP molecules across the dimer interface and by conformational rearrangements that position catalytic residues in each active site with respect to the bound substrate
light-harvesting chlorophyll a/b binding proteins are posttranslationally targeted to the thylakoid membrane by cpSRP, a heterodimer formed by cpSRP54 and cpSRP43
FlhF is dispensable for protein targeting and for growth and viability, it plays a minor role in cell motility, the flhF gene is located within the che/fla operon
FlhF is dispensable for protein targeting and for growth and viability, it plays a minor role in cell motility, the flhF gene is located within the che/fla operon
the sensor protein KdpD requires the signal recognition particle for its targeting to the membrane, small amphiphilic region of 27 residues within the amino-terminal domain of KdpD (amino acids 22-48) is recognized by SRP and targets the protein to the membrane, depletion of the Ffh component of SRP largely inhibits KdpD insertion
the sensor protein KdpD requires the signal recognition particle for its targeting to the membrane, small amphiphilic region of 27 residues within the amino-terminal domain of KdpD (amino acids 22-48) is recognized by SRP and targets the protein to the membrane, depletion of the Ffh component of SRP largely inhibits KdpD insertion