70,454 research outputs found
[{HC(CMeNAr)(2)}(2)Al2P4] (Ar=2,6-iPr(2)C(6)H(3)): A reduction to a formal {P-4},4(-) charged species
No full textPosttranslational modification of serine to formylglycine in bacterial sulfatases - Recognition of the modification motif by the iron-sulfur protein AtsB
Get PDFMarquordt C, Fang QH, Will E, Peng JH, Figura von K, Dierks T. Posttranslational modification of serine to formylglycine in bacterial sulfatases - Recognition of the modification motif by the iron-sulfur protein AtsB. JOURNAL OF BIOLOGICAL CHEMISTRY. 2003;278(4):2212-2218.Calpha-formylglycine is the catalytic residue of sulfatases. Formylglycine is generated by posttranslational modification of a cysteine (pro- and eukaryotes) or serine (pro-karyotes) located in a conserved (C/S)XPXR motif. The modifying enzymes are unknown. AtsB, an iron-sulfur protein, is strictly required for modification of Se-72 in the periplasmic sulfatase AtsA of Klebsiella pneumoniae. Here we show W that AtsB is a cytosolic protein acting on newly synthesized serine-type sulfatases, (ii) that AtsB-mediated FGly formation is dependent on AtsA's signal peptide, and (iii) that the cytosolic cysteine-type sulfatase of Pseudomonas aeruginosa can be converted into a substrate of AtsB if the cysteine is substituted by serine and a signal peptide is added. Thus, formylglycine formation in serine-type sulfatases depends both on AtsB and on the presence of a signal peptide, and AtsB can act on sulfatases of other species. AtsB physically interacts with AtsA in a Ser(72)-dependent manner, as shown in yeast two-hybrid and GST pulldown experiments. This strongly suggests that AtsB is the serine-modifying enzyme and that AtsB relies on a cytosolic function of the sulfatase's signal peptide
Letter from C. H. Gensler, Havasupai Agency to Carl Hayden
No full textLetter from C. H. Gensler expressing concern on behalf of the Havasupai Tribe regarding the proposed park boundaries
Citations of the author H C Rajpoot
No full textThe list of the articles, research papers, theses, and book chapters globally citing the author H. C. Rajpoot</p
Letter from Carl Hayden to C. H. Gensler
No full textLetter from Carl Hayden to C. H. Gensler informing him of the proposed Grand Canyon National Park bill
Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB
No full textFang QH, Peng JH, Dierks T. Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB. JOURNAL OF BIOLOGICAL CHEMISTRY. 2004;279(15):14570-14578.C-alpha-Formylglycine (FGly) is the catalytic residue of sulfatases. FGly is generated by post-translational modification of a cysteine ( prokaryotes and eukaryotes) or serine ( prokaryotes) located in a conserved (C/S) XPXR motif. AtsB of Klebsiella pneumoniae is directly involved in FGly generation from serine. AtsB is predicted to belong to the newly discovered radical S-adenosylmethionine (SAM) superfamily. By in vivo and in vitro studies we show that SAM is the critical co-factor for formation of a functional AtsB . SAM . sulfatase complex and for FGly formation by AtsB. The SAM-binding site of AtsB involves (83)GGE(85) and possibly also a juxtaposed FeS center coordinated by Cys(39) and Cys(42), as indicated by alanine scanning mutagenesis. Mutation of these and other conserved cysteines as well as treatment with metal chelators fully impaired FGly formation, indicating that all three predicted FeS centers are crucial for AtsB function. It is concluded that AtsB oxidizes serine to FGly by a radical mechanism that is initiated through reductive cleavage of SAM, thereby generating the highly oxidizing deoxyadenosyl radical, which abstracts a hydrogen from the serine-CbetaH2-OH side chain
Letter from C. H. Gensler, Havasupai Agency to Carl Hayden
No full textLetter from C. H. Gensler to Carl Hayden asking for a meeting in regards to the Havasupai pasture land in light of the national park bill
Synthesis and structural characterization of a terminal hydroxide containing alumoxane via hydrolysis of aluminum hydrides
No full textA novel terminal hydroxide containing dinuclear alumoxane LAl-(OH)OAlL(OCH=N-tBu) (3; L = HC(CMeNAr)(2), Ar = 2,6-iPr(2)C(6)H(3)) was prepared by treatment of aluminum dihydride LAlH2 (1) and tert-butyl isocyanate in the presence of trace amounts of water and alternatively from 1 and LAlH(OCH=N-tBu) (2) with water. Compound 2 was obtained from the reaction of 1 and tert-butyl isocyanate
Family ideals in an era of low fertility
No full textThis contains the dataset (.dta) and the replication dofile for "Family ideals in an era of low fertility" by Aassve A., Adserà, A., Chang, P.Y., Mencarini, L., Park, H., Peng, C., Plach, S., Raymo, J.M., Wang, S., & Yeung WJ
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