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Ubiquitous nuclear proteins bind to 5′ upstream region of major Kunitz chymotrypsin inhibitor gene in winged bean (1993)

Habu, Yoshiki ; Sakata, Yoichi ; Fukasawa, Kazuhiro ; [et al.]

Springer

Plant molecular biology 23 (1993), S. 1139-1150

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ISSN: 1573-5028

Keywords: DNA-binding proteins ; high mobility group proteins ; HMG proteins ; Kunitz proteinase inhibitor ; seed storage protein

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Winged bean Kunitz chymotrypsin inhibitor (WCI) accumulates abundantly in seeds and tuberous roots of winged bean plant. In seeds, the WCI mRNA is observed transiently during seed maturation period. The WCI is encoded by a multigene family and the major WCI (WCI-3) is encoded by two nearly identical genes (WCI-3a and WCI-3b genes), in which nucleotide sequences in the 1.1 kb 5′ flanking regions are about 99% homologous to each other and the transcribed regions are completely identical. Here we report the detection of two types of nuclear proteins which bind to the multiple sites in the 5′ upstream region of the WCI-3a gene. One of the proteins, band 1-forming protein, also bound to cauliflower mosaic virus 35S (CaMV35S) promoter, but another protein, band 3-forming protein, did not. DNaseI footprinting analysis showed that these proteins bound to AT-rich upstream regions in the WCI-3a gene. Addition of poly(dA-dT)-poly(dA-dT) to the binding reaction inhibited the formation of the retarded bands, while poly(dI-dC)-poly(dI-dC) did not. In various organs and throughout seed maturation period, proteins with invariable binding specificities were detected, and these binding proteins met some operational criteria for high-mobility-group (HMG) proteins. These results suggest that leguminous seed AT-binding proteins reported on several seed storage protein genes may be HMG-like proteins which are present ubiquitously in plant organs.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00042348

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Multiply charged ions of ruthenium(II), rhodium(III) and cobalt(III) complexes in electrospray ionization mass spectrometry (1994)

Arakawa, Ryuichi ; Matsuo, Takekiyo ; Ito, Hiroyuki ; [et al.]

Chichester : Wiley-Blackwell

Biological Mass Spectrometry 29 (1994), S. 289-294

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ISSN: 0030-493X

Keywords: Chemistry ; Analytical Chemistry and Spectroscopy

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology

Notes: Multiply charged ions from electrospray ionization (ESI) were observed for ruthenium-bidentate ligand complexes, such as [RuL2B]X2 and [(RuL2)2B]X4, where L is 2,2′-bipyridine, B are tetradentate ligands of 2,2′-bis(2′-pyridyl)bibenzimidazole and 2,6-bis(2′-pyridyl)benzodiimidazole, bidentate ligand of 2-(2′-pyridyl)benzimidazole and related compounds and X is CIO4- or CI-. ESI mass spectra showed a simple mass pattern for easy structural assignment and detecting impurities. The mass spectra for binuclear complexes provide a charge state distribution ranging from 4+ to 2+ for Ru(II) - Ru(II) compounds and 5+ to 2+ for Ru(II) - Rh(III) compounds. It was found that different multiply charged ions are generated by loss of counterions and by protonation/deprotonation at the proton site of ligands B. The abundances of these ions are qualitatively explained in terms of the acidity of metal complexes depending on the bridging ligand structures and the charge of the metal ions. Ions produced by removal of ligands were hardly observed.

Additional Material: 5 Ill.