Article Abstract:
The crystal structure of the two-subunit Oxytricha nova telomere end binding protein (OnTEBP) complexed with its telomeric single strand DNA-binding site is presented. The structure contains four folds that bind with oligonucleotide/oligosaccharide, three of which create a deep cleft binding the ssDNA. This structure offers a molecular characterization of a nucleoprotein complex that makes up the very end of a chromosome. It also describes the mechanism by which OnTEBP identifies, connects and protects telomeric DNA and shows how OnTEBP may control telomerase.
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Article Abstract:
Arabidopsis COP9 is a component of a large acidic protein complex that is necessary for the light control of a developmental switch. Light modulates the conformation or size of arabidopsis COP9. The complex, which binds heparin, is localized within the nucleus. It was found to contain 12 distinct subunits when biochemically purified to near homogeneity. The COP9 complex could represent a conserved developmental regulator in higher eukaryotes because both COP9 and COP11 have closely related human counterparts.
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Article Abstract:
The molecular interactions between the subunits constituting vertebrate and yeast transport protein particle (TRAPP 1) are analyzed. The identification of the minimal unit required for Ypt1 guanine nucleotide factor (GEF) activity and the architectural analysis of the complete TRAPP 1 tethering factor have helped in developing a model by which a complex imparts specificity in endoplasmic reticulum (ER)-to-Golgi traffic.
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