RT Journal Article
SR Electronic
T1 Disorder is a critical component of lipoprotein sorting in Gram-negative bacteria
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2021.01.05.425367
DO 10.1101/2021.01.05.425367
A1 Jessica El Rayes
A1 Joanna Szewczyk
A1 Michael Deghelt
A1 André Matagne
A1 Bogdan I. Iorga
A1 Seung-Hyun Cho
A1 Jean-François Collet
YR 2021
UL http://biorxiv.org/content/early/2021/01/05/2021.01.05.425367.abstract
AB Gram-negative bacteria express structurally diverse lipoproteins in their envelope. Here we found that approximately half of lipoproteins destined to the Escherichia coli outer membrane display an intrinsically disordered linker at their N-terminus. Intrinsically disordered regions are common in proteins, but establishing their importance in vivo has remained challenging. Here, as we sought to unravel how lipoproteins mature, we discovered that unstructured linkers are required for optimal trafficking by the Lol lipoprotein sorting system: linker deletion re-routes three unrelated lipoproteins to the inner membrane. Focusing on the stress sensor RcsF, we found that replacing the linker with an artificial peptide restored normal outer membrane targeting only when the peptide was of similar length and disordered. Overall, this study reveals the role played by intrinsic disorder in lipoprotein sorting, providing mechanistic insight into the biogenesis of these proteins and suggesting that evolution can select for intrinsic disorder that supports protein function.Competing Interest StatementThe authors have declared no competing interest.