A Nonessential Sfp-Type Phosphopantetheinyl Transferase Contributes Significantly to the Pathogenicity of .

Phytopathology

Guangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou, Guangdong 510642, China.

Published: November 2024


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Article Abstract

4'-Phosphopantetheinyl transferases (PPTases) play important roles in the posttranslational modifications of bacterial carrier proteins, which are involved in various metabolic pathways. Here, we found that and encoded a functional AcpS-type and Sfp-type PPTase, respectively, in GMI1000, and both are capable of modifying AcpP1, AcpP2, AcpP3, and AcpP5 proteins. is located on the megaplasmid, which does not affect strain growth and fatty acid synthesis but significantly contributes to the virulence of and preferentially participates in secondary metabolism. We found that deletion of did not affect the abilities of cellulose degradation, biofilm formation, and resistance to NaCl, sodium dodecyl sulfate, and HO and attenuated pathogenicity only in the assay of soil-drenching infection but not stem injection of tomato. It is hypothesized that RsPcpS plays a role in cell viability in complex environments and in the process during which the strain recognizes and approaches plants. These results suggest that both RsAcpS and RsPcpS may be potential targets for controlling diseases caused by .

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http://dx.doi.org/10.1094/PHYTO-04-24-0113-RDOI Listing

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A Nonessential Sfp-Type Phosphopantetheinyl Transferase Contributes Significantly to the Pathogenicity of .

Phytopathology

November 2024

Guangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou, Guangdong 510642, China.

4'-Phosphopantetheinyl transferases (PPTases) play important roles in the posttranslational modifications of bacterial carrier proteins, which are involved in various metabolic pathways. Here, we found that and encoded a functional AcpS-type and Sfp-type PPTase, respectively, in GMI1000, and both are capable of modifying AcpP1, AcpP2, AcpP3, and AcpP5 proteins. is located on the megaplasmid, which does not affect strain growth and fatty acid synthesis but significantly contributes to the virulence of and preferentially participates in secondary metabolism.

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