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Significance Many water-soluble proteins are known to fold and even dimerize cotranslationally (i.e., when still attached to the ribosome). However, it has proven difficult to ascertain whether transmembrane α-helices in… Click to show full abstract
Significance Many water-soluble proteins are known to fold and even dimerize cotranslationally (i.e., when still attached to the ribosome). However, it has proven difficult to ascertain whether transmembrane α-helices in an integral membrane protein can interact cotranslationally and whether membrane proteins can start to dimerize while still being synthesized. Here, we show that a model Escherichia coli inner membrane protein appears to be able to start to fold and dimerize cotranslationally in vivo, suggesting the generality of these cotranslational maturation processes.
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Year Published: 2022
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