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University of Connecticut

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2013

Amphipathic membrane binding domain

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Full-Text Articles in Medicine and Health Sciences

Membrane Association Via An N-Terminal Amphipathic Helix Is Required For The Cellular Organization And Function Of Rnase Ii, Feng Lu, Aziz Taghbalout Jan 2013

Membrane Association Via An N-Terminal Amphipathic Helix Is Required For The Cellular Organization And Function Of Rnase Ii, Feng Lu, Aziz Taghbalout

UCHC Articles - Research

The subcellular localization of the exoribonuclease RNase II is not known despite the advanced biochemical characterization of the enzyme. Here we report that RNase II is organized into cellular structures that appear to coil around the Escherichia coli cell periphery and that RNase II is associated with the cytoplasmic membrane by its aminoterminal amphipathic helix. The helix also acts as an autonomous transplantable membranebinding domain capable of directing normally cytoplasmic proteins to the membrane. Assembly of the organized cellular structures of RNase II required the RNase II amphipathic membrane-binding domain. Coimmunoprecipitation of the protein from cell extracts indicated that RNase …