A Maize (Zea mays L.) BIK1-Like Receptor-Like Cytoplasmic Kinase Contributes to Disease Resistance
Receptor-like cytoplasmic kinases (RLCKs) form a large subfamily of proteins in plants. RLCKs are known to regulate plant immunity to bacterial and fungal pathogens. In this study, we analyzed the genome-wide complement of maize RLCK genes and conducted detailed studies on one maize RLCK. The maize...
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Veröffentlicht in: | Plant molecular biology reporter 2022-03, Vol.40 (1), p.28-42 |
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Zusammenfassung: | Receptor-like cytoplasmic kinases (RLCKs) form a large subfamily of proteins in plants. RLCKs are known to regulate plant immunity to bacterial and fungal pathogens. In this study, we analyzed the genome-wide complement of maize RLCK genes and conducted detailed studies on one maize RLCK. The maize genome encodes 192 RLCKs that largely mirror the RLCK family in other plants. Previous studies implicated Arabidopsis BOTRYTIS INDUCED KINASE1 (BIK1) and TOMATO PROTEIN KINASE 1b (TPK1b) in plant resistance to the bacterial pathogen
Pseudomonas syringae
and the fungal pathogen
Botrytis cinerea
. A novel maize RLCK,
Zea Mays BIK1-LIKE KINASE 1 (ZmBLK1)
, was identified based on sequence similarity to the tomato and Arabidopsis RLCKs. We demonstrated that ZmBLK1 displays protein kinase activity in vitro and the protein localizes to the plasma membrane. Importantly, expression of
ZmBLK1
partially rescued the growth and disease phenotypes of the Arabidopsis
bik1
mutant plants. The expression of
ZmBLK1
was induced in maize at 12 h after inoculation with
Clavibacter michiganensis
subsp.
nebraskensis
(CMN), the bacterial pathogen causing Goss’s wilt. Interestingly, overexpression of
ZmBLK1
in transgenic maize increased resistance to CMN but did not impact resistance to Aspergillus ear rot caused by the fungal pathogen
Aspergillus flavus
and the associated aflatoxin contamination. These findings support our hypothesis that
ZmBLK1
contributes to plant resistance to bacterial pathogens likely by modulating events early after pathogen infection, implying that the protein may interact with other membrane proteins early in the immune response pathway. |
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ISSN: | 0735-9640 1572-9818 |
DOI: | 10.1007/s11105-021-01299-2 |