Universal flux-fluctuation law in small systems

We thank Dr. DeMenezes for providing the microchip data. This work was partially supported by the NSF of China under Grant Nos. 11135001, 11275003. Y.C.L. was supported by ARO under Grant No. W911NF-14-1-0504.Peer reviewedPublisher PD

6-(4-Fluoro­pheneth­yl)-7-imino-3-phenyl-2,3,6,7-tetra­hydro-1,3-thia­zolo[4,5-d]pyrimidine-2-thione

In the title compound, C19H15FN4S2, the mean plane of the thia­zolopyrimidine makes a dihedral angle of 77.6 (1)° with the attached phenyl ring. The crystal packing is stabilized by inter­molecular C—H⋯N hydrogen bonds and weak C—H—π stacking inter­actions

(E)-(2-Chloro­benzyl­idene)amino 2-amino-4-chloro­benzoate

In the title compound, C14H10Cl2N2O2, the configuration about the C=N double bond is E and the dihedral angle between the benzene rings is 1.75 (5)°. An intra­molecular N—H⋯O inter­action generates an S(6) ring. In the crystal, mol­ecules are linked by N—H⋯O hydrogen bonds, resulting in [101] chains

The juxtamembrane and carboxy-terminal domains of Arabidopsis PRK2 are critical for ROP-induced growth in pollen tubes.

Polarized growth of pollen tubes is a critical step for successful reproduction in angiosperms and is controlled by ROP GTPases. Spatiotemporal activation of ROP (Rho GTPases of plants) necessitates a complex and sophisticated regulatory system, in which guanine nucleotide exchange factors (RopGEFs) are key components. It was previously shown that a leucine-rich repeat receptor-like kinase, Arabidopsis pollen receptor kinase 2 (AtPRK2), interacted with RopGEF12 for its membrane recruitment. However, the mechanisms underlying AtPRK2-mediated ROP activation in vivo are yet to be defined. It is reported here that over-expression of AtPRK2 induced tube bulging that was accompanied by the ectopic localization of ROP-GTP and the ectopic distribution of actin microfilaments. Tube depolarization was also induced by a potentially kinase-dead mutant, AtPRK2K366R, suggesting that the over-expression effect of AtPRK2 did not require its kinase activity. By contrast, deletions of non-catalytic domains in AtPRK2, i.e. the juxtamembrane (JM) and carboxy-terminal (CT) domains, abolished its ability to affect tube polarization. Notably, AtPRK2K366R retained the ability to interact with RopGEF12, whereas AtPRK2 truncations of these non-catalytic domains did not. Lastly, it has been shown that the JM and CT domains of AtPRK2 were not only critical for its interaction with RopGEF12 but also critical for its distribution at the plasma membrane. These results thus provide further insight into pollen receptor kinase-mediated ROP activation during pollen tube growth

N-[3,5-Dichloro-4-(1,1,2,2-tetra­fluoro­eth­oxy)phen­yl]-2,6-difluoro­benzamide

In the title compound, C15H7Cl2F6NO2, the conformation of the N—H bond in the amide segment is anti to the C=O bond and the dihedral angle between the two benzene rings is 78.6 (3)°. The terminal –CHF2 group is disordered over two orientations in a 0.67:0.33 ratio. In the crystal, the mol­ecules are linked by N—H⋯O hydrogen bonds, generating C(4) chains propagating in [100]

Complex behavior of chaotic synchronization under dual coupling channels

We thank an anonymous referees for substantial and constructing comments. This work was partially supported by NSF of China under Grants No. 91026005, No. 11135001, No. 11275003, No. 11375109, No. 11422541, and No. 11375074, and by the Fundamental Research Funds for the Central Universities under Grant Nos. GK201303002 and lzujbky-2014-33. YCL was supported by ONR under Grant No. N00014-08-1-0627.Peer reviewedPublisher PD