A signal peptide peptidase is required for ER-symbiosome proximal association and protein secretion

Jian Yang, Niu Zhai, Yuhui Chen, Luying Wang, Rujin Chen and Huairong Pan ()
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Jian Yang: Hunan University
Niu Zhai: Zhengzhou Tobacco Research Institute of CNTC
Yuhui Chen: Lanzhou University
Luying Wang: Hunan University
Rujin Chen: Lanzhou University
Huairong Pan: Hunan University

Nature Communications, 2023, vol. 14, issue 1, 1-11

Abstract: Abstract During legume-rhizobia symbiosis, differentiation of the symbiosome (engulfed intracellular rhizobia) is necessary for successful nitrogen fixation. To control symbiosome differentiation, host cell subcellular components, e.g., ER (endoplasmic reticulum), must adapt robustly to ensure large-scale host protein secretion to the new organelle. However, the key components controlling the adaption of ER in nodule cells remain elusive. We report that Medicago BID1, a nodule-specific signal peptide peptidase (SPP), is central to ER structural dynamics and host protein secretion. In bid1, symbiosome differentiation is blocked. BID1 localizes specifically to the ER membrane and expresses exclusively in nodule cells with symbiosomes. In the wild type ER forms proximal association structures with symbiosomes, but not in bid1. Consequently, in bid1 excessive ER stress responses are induced and ER-to-symbiosome protein secretion is impaired. In summary, a nodule-specific SPP is necessary for ER-symbiosome proximal association, host protein secretion, and symbiosome differentiation.

Date: 2023
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DOI: 10.1038/s41467-023-40008-3

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