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TyeA, a protein involved in control of Yop release and in translocation of Yersinia Yop effectors
Author(s) -
Iriarte Maite,
Sory MariePaule,
Boland Anne,
Boyd Aoife P.,
Mills Scott D.,
Lambermont Isabelle,
Cornelis Guy R.
Publication year - 1998
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/17.7.1907
Subject(s) - biology , effector , chromosomal translocation , yersinia , microbiology and biotechnology , bacterial protein , bacteria , genetics , gene
Extracellular Yersinia spp. disarm the immune system by injecting the effector Yersinia outer proteins (Yops) into the target cell. Yop secretion is triggered by contact with eukaryotic cells or by Ca 2+ chelation. Two proteins, YopN and LcrG, are known to be involved in Yop‐secretion control. Here we describe TyeA, a third protein involved in the control of Yop release. Like YopN, TyeA is localized at the bacterial surface. A tyeA knock‐out mutant secreted Yops in the presence of Ca 2+ and in the absence of eukaryotic cells. Unlike a yopN null mutant, the tyeA mutant was defective for translocation of YopE and YopH, but not YopM, YopO and YopP, into eukaryotic cells. This is the first observation suggesting that Yop effectors can be divided into two sets for delivery into eukaryotic cells. TyeA was found to interact with the translocator YopD and with residues 242–293 of YopN. In contrast with a yopN null mutant, a yopN Δ248–272 mutant was also unable to translocate YopE and YopH. Our results suggest that TyeA forms part of the translocation‐control apparatus together with YopD and YopN, and that the interaction of these proteins is required for selective translocation of Yops inside eukaryotic cells.