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Biochem Soc Trans. 2019 Feb 1. pii: BST20180543. doi: 10.1042/BST20180543. [Epub ahead of print]

Emerging paradigms for PilZ domain-mediated C-di-GMP signaling.

Author information

1
School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, S637551 Singapore.
2
School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, S637551 Singapore zxliang@ntu.edu.sg.

Abstract

PilZ domain-containing proteins constitute a large family of bacterial signaling proteins. As a widely distributed protein domain for the binding of the second messenger c-di-GMP, the canonical PilZ domain contains a set of motifs that define the binding site for c-di-GMP and an allosteric switch for propagating local conformational changes. Here, we summarize some new insights gathered from recent studies on the commonly occurring single-domain PilZ proteins, YcgR-like proteins and PilZ domain-containing cellulose synthases. The studies collectively illuminate how PilZ domains function as cis- or trans-regulatory domains that enable c-di-GMP to control the activity of its cellular targets. Overall, the review highlights the diverse protein structure, biological function and regulatory mechanism of PilZ domain-containing proteins, as well as the challenge of deciphering the function and mechanism of orphan PilZ proteins.

KEYWORDS:

PilZ domain; allosteric regulation; cellulose synthase; cyclic di-GMP; flagella; protein–protein interactions

PMID:
30710060
DOI:
10.1042/BST20180543

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