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cAMP 和 c-di-GMP 通过其效应物的直接相互作用协同支持生物膜的维持。

cAMP and c-di-GMP synergistically support biofilm maintenance through the direct interaction of their effectors.

机构信息

Jiangsu Key Laboratory of Phylogenomics & Comparative Genomics, School of Life Sciences, Jiangsu Normal University, Xuzhou, China.

出版信息

Nat Commun. 2022 Mar 21;13(1):1493. doi: 10.1038/s41467-022-29240-5.

DOI:10.1038/s41467-022-29240-5
PMID:35315431
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8938473/
Abstract

Nucleotide second messengers, such as cAMP and c-di-GMP, regulate many physiological processes in bacteria, including biofilm formation. There is evidence of cross-talk between pathways mediated by c-di-GMP and those mediated by the cAMP receptor protein (CRP), but the mechanisms are often unclear. Here, we show that cAMP-CRP modulates biofilm maintenance in Shewanella putrefaciens not only via its known effects on gene transcription, but also through direct interaction with a putative c-di-GMP effector on the inner membrane, BpfD. Binding of cAMP-CRP to BpfD enhances the known interaction of BpfD with protease BpfG, which prevents proteolytic processing and release of a cell surface-associated adhesin, BpfA, thus contributing to biofilm maintenance. Our results provide evidence of cross-talk between cAMP and c-di-GMP pathways through direct interaction of their effectors, and indicate that cAMP-CRP can play regulatory roles at the post-translational level.

摘要

核苷酸第二信使,如 cAMP 和 c-di-GMP,调节细菌中的许多生理过程,包括生物膜的形成。有证据表明,c-di-GMP 介导的途径与 cAMP 受体蛋白 (CRP) 介导的途径之间存在串扰,但机制通常不清楚。在这里,我们表明 cAMP-CRP 通过其对基因转录的已知作用,以及通过与内膜上假定的 c-di-GMP 效应物 BpfD 的直接相互作用,不仅调节腐生脱硫肠弧菌的生物膜维持,还调节生物膜维持。cAMP-CRP 与 BpfD 的结合增强了 BpfD 与蛋白酶 BpfG 的已知相互作用,从而阻止了细胞表面相关粘附素 BpfA 的蛋白水解加工和释放,从而有助于生物膜的维持。我们的结果提供了 cAMP 和 c-di-GMP 途径通过其效应物的直接相互作用进行串扰的证据,并表明 cAMP-CRP 可以在翻译后水平发挥调节作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c75a/8938473/2078771fbcd6/41467_2022_29240_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c75a/8938473/26641c26bd92/41467_2022_29240_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c75a/8938473/3a97d05dcf36/41467_2022_29240_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c75a/8938473/9f554fe47a76/41467_2022_29240_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c75a/8938473/5d2a10d4de50/41467_2022_29240_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c75a/8938473/7b668cde219f/41467_2022_29240_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c75a/8938473/2078771fbcd6/41467_2022_29240_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c75a/8938473/26641c26bd92/41467_2022_29240_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c75a/8938473/3a97d05dcf36/41467_2022_29240_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c75a/8938473/9f554fe47a76/41467_2022_29240_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c75a/8938473/5d2a10d4de50/41467_2022_29240_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c75a/8938473/7b668cde219f/41467_2022_29240_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c75a/8938473/2078771fbcd6/41467_2022_29240_Fig6_HTML.jpg

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