Structural Characterization of Maize SIRK1 Kinase Domain Reveals an Unusual Architecture of the Activation Segment

Aquino, Bruno; Couñago, Rafael M.; Verza, Natalia; Ferreira, Lucas M.; Massirer, Katlin B.; Gileadi, Opher; Arruda, Paulo

doi:10.3389/fpls.2017.00852

Structural Characterization of Maize SIRK1 Kinase Domain Reveals an Unusual Architecture of the Activation Segment

Journal Article · Fri May 26 00:00:00 EDT 2017 · Frontiers in Plant Science

DOI:https://doi.org/10.3389/fpls.2017.00852· OSTI ID:1430299

Aquino, Bruno ^[1]; Couñago, Rafael M. ^[1]; Verza, Natalia ^[1]; Ferreira, Lucas M. ^[1]; Massirer, Katlin B. ^[1]; Gileadi, Opher ^[2]; Arruda, Paulo ^[1]

Univ. Estadual de Campinas (Brazil)
Univ. Estadual de Campinas (Brazil); Univ. of Oxford (United Kingdom)

Kinases are primary regulators of plant metabolism and excellent targets for plant breeding. However, most kinases, including the abundant receptor-like kinases (RLK), have no assigned role. SIRK1 is a leucine-rich repeat receptor-like kinase (LRR-RLK), the largest family of RLK. In Arabidopsis thaliana, SIRK1 (AtSIRK1) is phosphorylated after sucrose is resupplied to sucrose-starved seedlings and it modulates the sugar response by phosphorylating several substrates. In maize, the ZmSIRK1 expression is altered in response to drought stress. In neither Arabidopsis nor in maize has the function of SIRK1 been completely elucidated. As a first step toward the biochemical characterization of ZmSIRK1, we obtained its recombinant kinase domain, demonstrated that it binds AMP-PNP, a non-hydrolysable ATP-analog, and solved the structure of ZmSIRK1- AMP-PNP co-crystal. The ZmSIRK1 crystal structure revealed a unique conformation for the activation segment. In an attempt to find inhibitors for ZmSIRK1, we screened a focused small molecule library and identified six compounds that stabilized ZmSIRK1 against thermal melt. ITC analysis confirmed that three of these compounds bound to ZmSIRK1 with low micromolar affinity. Solving the 3D structure of ZmSIRK1-AMP-PNP co-crystal provided information on the molecular mechanism of ZmSIRK1 activity. Furthermore, the identification of small molecules that bind this kinase can serve as initial backbone for development of new potent and selective ZmSIRK1 antagonists.

View Accepted Manuscript (DOE)

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: USDOE Office of Science (SC); Sao Paulo Research Foundation

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1430299

Journal Information:: Frontiers in Plant Science, Journal Name: Frontiers in Plant Science Journal Issue: 05, 2017 Vol. 8; ISSN 1664-462X

Publisher:: Frontiers Research FoundationCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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59 BASIC BIOLOGICAL SCIENCES
SIRK1
ligand
maize
receptor-like kinase
structure

Structural Characterization of Maize SIRK1 Kinase Domain Reveals an Unusual Architecture of the Activation Segment

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