Motif N (motif + n)

Distribution by Scientific Domains


Selected Abstracts


Insecticidal action of mammalian galectin-1 against diamondback moth (Plutella xylostella)

PEST MANAGEMENT SCIENCE (FORMERLY: PESTICIDE SCIENCE), Issue 8 2009
Shiang Jiuun Chen
Abstract BACKGROUND: Previous studies showed that mammalian galectin-1 (GAL1) could interact with chitosan or chitin, one component of the peritrophic membrane (PM). This finding suggests that the PM could be a target of GAL1, which prompted the authors to explore the effect of GAL1 on larval growth and its potential mechanism. RESULTS: The development of Plutella xylostella (L.) larvae was significantly disturbed after they were fed recombinant GAL1. The histochemical structure and immunostaining pattern suggested that GAL1 treatment resulted in dose- and time-dependent disruption of the microvilli and abnormalities in these epithelial cells. Ultrastructural studies showed that the PM was not present in the midgut of GAL1-treated insects; instead, numerous bacteria were found in the lumen area. These results indicate that the protective function of the PM was disrupted by GAL1 treatment. Moreover, in vitro data showed that GAL1 interacts with chitosan/chitin in a dose-dependent manner, and also specifically binds to the PM in vitro. CONCLUSION: In view of the fact that the carbohydrate recognition domain of GAL1 recognises the structural motif N -acetyl lactosamine (Gal , 1,4 GlcNAc), which is similar to that of chitin (,-1,4 N -acetyl- D -glucosamine), it is proposed that the insecticidal mechanism of GAL1 involves direct binding with chitin to interfere with the structure of the PM. Copyright 2009 Society of Chemical Industry [source]


Crystallization and preliminary X-ray diffraction analysis of motif N from Saccharomyces cerevisiae Dbf4

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 9 2009
Lindsay A. Matthews
The Cdc7,Dbf4 complex plays an instrumental role in the initiation of DNA replication and is a target of replication-checkpoint responses in Saccharomyces cerevisiae. Cdc7 is a conserved serine/threonine kinase whose activity depends on association with its regulatory subunit, Dbf4. A conserved sequence near the N-terminus of Dbf4 (motif N) is necessary for the interaction of Cdc7,Dbf4 with the checkpoint kinase Rad53. To understand the role of the Cdc7,Dbf4 complex in checkpoint responses, a fragment of Saccharomyces cerevisiae Dbf4 encompassing motif N was isolated, overproduced and crystallized. A complete native data set was collected at 100,K from crystals that diffracted X-rays to 2.75, resolution and structure determination is currently under way. [source]