The motor function of Drosophila melanogaster myosin-5 is activated by calcium and cargo-binding protein dRab11

2015 ◽  
Vol 469 (1) ◽  
pp. 135-144 ◽  
Author(s):  
Huan-Hong Ji ◽  
Hai-Man Zhang ◽  
Mei Shen ◽  
Lin-Lin Yao ◽  
Xiang-dong Li
Keyword(s):  
Drosophila Melanogaster ◽  
Motor Function ◽  
Binding Protein ◽  
Cargo Binding

We demonstrated that the motor function of Drosophila melanogaster myosin-5 (DmM5) is stimulated by calcium and cargo-binding protein dRab11, but not by cargo-binding protein Lightoid (Ltd).

scholarly journals Activation of Drosophila Melanogaster Myosin-5 Motor Function by Calcium and Cargo-Binding Protein

2015 ◽  
Vol 108 (2) ◽  
pp. 302a-303a
Author(s):  
Huan-Hong Ji ◽  
Hai-Man Zhang ◽  
Mei Shen ◽  
Xiang-dong Li
Keyword(s):  
Drosophila Melanogaster ◽  
Motor Function ◽  
Binding Protein ◽  
Cargo Binding

Banding patterns in Drosophila melanogaster polytene chromosomes correlate with DNA-binding protein occupancy

BioEssays ◽  
2012 ◽  
Vol 34 (6) ◽  
pp. 498-508 ◽  
Author(s):  
Igor F. Zhimulev ◽  
Elena S. Belyaeva ◽  
Tatiana Yu Vatolina ◽  
Sergey A. Demakov
Keyword(s):  
Drosophila Melanogaster ◽  
Dna Binding ◽  
Binding Protein ◽  
Polytene Chromosomes ◽  
Dna Binding Protein ◽  
Banding Patterns ◽  
Protein Occupancy

scholarly journals Natural Variation, Functional Pleiotropy and Transcriptional Contexts of Odorant Binding Protein Genes in Drosophila melanogaster

Genetics ◽  
2010 ◽  
Vol 186 (4) ◽  
pp. 1475-1485 ◽  
Author(s):  
Gunjan H. Arya ◽  
Allison L. Weber ◽  
Ping Wang ◽  
Michael M. Magwire ◽  
Yazmin L. Serrano Negron ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Natural Variation ◽  
Binding Protein ◽  
Odorant Binding Protein ◽  
Odorant Binding

scholarly journals Cargo binding activates myosin VIIA motor function in cells

2011 ◽  
Vol 108 (17) ◽  
pp. 7028-7033 ◽  
Author(s):  
T. Sakai ◽  
N. Umeki ◽  
R. Ikebe ◽  
M. Ikebe
Keyword(s):  
Motor Function ◽  
Myosin Viia ◽  
In Cells ◽  
Cargo Binding

scholarly journals H3K27 modifications define segmental regulatory domains in the Drosophila bithorax complex

eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Sarah K Bowman ◽  
Aimee M Deaton ◽  
Heber Domingues ◽  
Peggy I Wang ◽  
Ruslan I Sadreyev ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Binding Protein ◽  
Histone H3 ◽  
Polycomb Group ◽  
Homeotic Genes ◽  
Bithorax Complex ◽  
Body Segment ◽  
Regulatory Domains ◽  
Definition Of ◽  
Identity Expression

The bithorax complex (BX-C) in Drosophila melanogaster is a cluster of homeotic genes that determine body segment identity. Expression of these genes is governed by cis-regulatory domains, one for each parasegment. Stable repression of these domains depends on Polycomb Group (PcG) functions, which include trimethylation of lysine 27 of histone H3 (H3K27me3). To search for parasegment-specific signatures that reflect PcG function, chromatin from single parasegments was isolated and profiled. The H3K27me3 profiles across the BX-C in successive parasegments showed a ‘stairstep’ pattern that revealed sharp boundaries of the BX-C regulatory domains. Acetylated H3K27 was broadly enriched across active domains, in a pattern complementary to H3K27me3. The CCCTC-binding protein (CTCF) bound the borders between H3K27 modification domains; it was retained even in parasegments where adjacent domains lack H3K27me3. These findings provide a molecular definition of the homeotic domains, and implicate precisely positioned H3K27 modifications as a central determinant of segment identity.

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