Divalent cation-nucleotide complex at the exchangeable nucleotide binding site of tubulin.
نویسندگان
چکیده
منابع مشابه
Binding of fluorescent analogs of GTP to the exchangeable nucleotide binding site of tubulin.
6 S tubulin from which the exchangeably bound guanine nucleotide had been removed was examined for its ability to bind two fluorescent analogs of GTP. One analog, (y-AmNS)GTP, contains the fluorophore l-aminonaphthalene 5-sulfonate attached to the y phosphate of GTP via a phosphoamidate bond. The second analog contains the same fluorophore attached to the sulfur atom of GTP-y-S via a 5-atom lin...
متن کاملآنالیز پروفایل nbs (nucleotide binding-site) ژنهای مقاومت به بیماری در ارقام مختلف زیتون
به منظور مطالعه ژنهای مقاومت nbs-lrr و تنوع ژنتیکی آنها در بین ارقام بومی زیتون و همچنین مقایسه آن با ارقام خارجی، از تکنیک profiling nbs و آنالیزهای مولکولی استفاده شد. برای این منظور dna ژنومی تعداد 5 رقم خارجی و 5 رقم داخلی زیتون استخراج و با آنزیم های برشی alui و rsai هضم و با استفاده از 3 آغازگر دژنره( nbs2،nbs7،nbs5a) در دو مرحله تکثیر شدند و الگوی باندی حاصل از تکثیر انتخابی آنها در روی ...
Divalent cation transport by VNUT DIVALENT CATION TRANSPORT BY VESICULAR NUCLEOTIDE TRANSPORTER
The vesicular nucleotide transporter (VNUT) is a secretory vesicle protein that is responsible for the vesicular storage and subsequent exocytosis of ATP (Sawada, K. et al., (2008) Proc. Natl. Acad. Sci. U.S.A. 105, 11720-11724). Since VNUT actively transports ATP in a membrane potential (Δψ)-dependent manner irrespective of divalent cations such as Mg or Ca, VNUT recognizes free ATP as a trans...
متن کاملBinding of dolastatin 10 to tubulin at a distinct site for peptide antimitotic agents near the exchangeable nucleotide and vinca alkaloid sites.
Dolastatin 10, a potent antimitotic peptide from a marine animal, strongly inhibits microtubule assembly, tubulin-dependent GTP hydrolysis, and the binding of vinca alkaloids to tubulin. In studies of the binding of [3H]vincristine to the protein, with vinblastine as a control for competitive inhibition (Ki, 6.6 microM), we found that the macrolide antimitotic agents maytansine and rhizoxin wer...
متن کاملInteraction of tubulin with ribose-modified analogs of GTP and GDP: evidence for two mutually exclusive exchangeable nucleotide binding sites.
Interactions of tubulin with a number of guanine nucleotides modified at the 2' and 3' ribose hydroxyls were examined. Deoxy analogs of GTP were equal or superior to GTP in supporting tubulin polymerization, but analogs bearing either methyl or phosphate groups on the hydroxyls had significantly reduced ability to support polymerization. These substituted GTP analogs were hydrolyzed at the 5'-g...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1982
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)34309-6