Interaction of actinogelin with actin. No nucleation but high gelation activity
نویسندگان
چکیده
منابع مشابه
Rab1 recruits WHAMM during membrane remodeling but limits actin nucleation
Small G-proteins are key regulatory molecules that activate the actin nucleation machinery to drive cytoskeletal rearrangements during plasma membrane remodeling. However, the ability of small G-proteins to interact with nucleation factors on internal membranes to control trafficking processes has not been well characterized. Here we investigated roles for members of the Rho, Arf, and Rab G-pro...
متن کاملActin polymerization and interaction with other proteins in temperature- induced gelation of sea urchin egg extracts
The gel which forms on warming the extracts of the cytoplasmic proteins of sea urchin eggs has been separated into two fractions, one containing F-actin and the other containing two proteins of 58,000 and 22,000 mol wt. When combined in 0.1 M KCl, even at 0 degrees C, these components will form gel material identical to that formed by warming extracts. This gel is a network of laterally aggrega...
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برهمکنش dnaتیموس گاوی طبیعی (ct-dna) با اتیلن دی آمین تترااستات (edta)در بافرtris-hcl با 8/7 ph ( دراین ph،edta به نمک دی سدیم تبدیل می شود) وسسامول در بافر tris-hcl با4/7 ph مورد بررسی قرار گرفته است. edta و سسامول استفاده فراوانی در تکنولوژی غذایی و صنعت شیمیایی دارند. مدل اتصال dna مربوط بهedta بوسیله اسپکتروفتومتری جذب، دورنگ نمایی حلقوی(cd)، ویسکومتری وژل الکتروفورز بررسی شده است. طیفuv ...
15 صفحه اولCharacterization and localization of actinogelin, a Ca2+ - sensitive actin accessory protein, in nonmuscle cells
Actinogelin, which induces gelation of F-actin at Ca2+ concentrations below micromolar concentrations but not at higher concentrations, was isolated in the pure state from Ehrlich tumor cells. The protein consists of subunits of 112,000-115,000 daltons and under physiological conditions is present mostly as a dimer. Up to 1 mol of actinogelin (dimer) binds to 10-12 mol of actin monomer. The bin...
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We have studied the abundance, relative gelation activity, and distribution of the 95,000-dalton actin-binding protein in Dictyostelium discoideum amoebae. The 95,000-dalton protein was a prominent polypeptide as assessed using quantitative densitometry and radioimmunoassay. We estimated that this protein comprised approximately 1.2% of the protein in a soluble extract of amoebae. The molar rat...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1985
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1985.tb09344.x