Disease relevance of LOC540432

• A 14-amino acid arginine-rich peptide corresponding to the RNA-binding domain of BIV Tat binds specifically to BIV TAR, and biochemical and in vivo experiments have identified the amino acids and nucleotides required for binding [1].
• By contrast, the amino terminus of N, the acidic carboxy-terminal domain, and a serine- and arginine-rich segment of the central domain could not be transferred from bovine coronavirus to MHV, presumably because these parts of the molecule participate in protein-protein interactions that are specific for each virus (or, possibly, each host) [2].

High impact information on LOC540432

• The primary structure of mammalian protamine I can be divided into three domains, a central DNA binding domain that is arginine-rich and amino- and carboxyl-terminal domains that are rich in cysteine residues [3].
• Phosphatidylinositol (4,5)-bisphosphate-dependent activation of dynamins I and II lacking the proline/arginine-rich domains [4].
• Bac5 is a 5-kDa proline- and arginine-rich antibiotic, stored as inactive precursor (proBac5) in the large granules of bovine neutrophils [5].
• Only cyclic GMP bound to the high affinity site (Site I) correlated with stimulation of histone kinase activity using arginine-rich histone as the substrate; however, both sites were involved with stimulation of histone kinase activity using mixed histones as the substrate [6].
• A nucleosome-like structure containing DNA and the arginine-rich histones H3 and H4 [7].

Biological context of LOC540432

• Biochemical, spectroscopic, and hydrodynamic studies were performed on the reconstituted complex of 140 base pair DNA and the arginine-rich histone tetramer (H3/H4)2 [8].
• Nonenzymatic acetylation of calf-thymus lysine- and arginine-rich histones was demonstrated to occur when these proteins were incubated with [14C]acetyl phosphate and [14C]acetyl adenylate [9].
• PEM lysates were analyzed for PKC-alpha mRNA (Northern cDNA blot), protein (Western immunoblot), and activity (translocation and phosphorylation of myristoylated arginine-rich C kinase substrate) [10].
• The protein substrate specificity was in the order histone greater than arginine-rich histone greater than casein greater than protamine greater than lysine-rich histone [11].
• The different hydrolysis kinetics of chromatin of blood-sucking insect spermatozoa compared to that of grasshopper, sea-urchin, and bee sperm cells suggests that, although the first 2 materials contain an arginine-rich "germinative" protein and the latter 2 ones contain a lysine-rich protein, these differ to each other [12].

Anatomical context of LOC540432

• Two histones from calf thymus, the slightly lysine-rich histone f2a2 and the arginine-rich f3, were combined separately, with homologous DNA [13].
• ARP turnover by the lens fiber cell Na,K-ATPase (1700 +/- 600 min-1) was lower than ATP turnover by the lens epithelium Na,K-ATPase (8000 +/0 1000 min-1) [14].
• Inhibition of mammary gland cyclic AMP-dependent protein kinase by arginine-rich histones [15].
• Although the slightly lysine-rich and the arginine-rich histones in Oxytricha macronuclei are similar to comparable fractions in vertebrates, the lysine-rich f1 fraction differs [16].
• The Km values of the solubilized myelin fraction were 4.2 muM for myelin basic protein, 7.4 muM for arginine-rich histone, 8.0 muM for histone mixture and 14.3 muM for protamine, respectively [17].

Associations of LOC540432 with chemical compounds

• Thus, the arginine-rich histones and the tightly bound non-histones are most responsible for limiting the binding of ethidium bromide to rye chromatin [18].
• Lysine-rich and arginine-rich histones serve as the most effective exogenous protein acceptors; P. polycephalum actomyosin is inactive, and chick skeletal myofibrillar proteins are 25% as effective as exogenous mixed histones as substrates [19].
• N(G)-Methylation of arginine residues in many nucleic-acid-binding proteins are formed post-translationally, catalysed by S-adenosylmethionine:protein-arginine N-methyltransferase in their glycine-rich and arginine-rich motifs [20].
• Furthermore, only a small amount of O-bound radioactivity was released by the 14C-labeled acetylated arginine-rich histone during treatment with hydroxylamine [9].
• In the case of arginine-rich histones H3 (III or f3) and H4 (IV or f2a1), four methods were used for making complexes with calf thymus DNA: (A) NaCl gradient dialysis with urea; (B) NaCl gradient dialysis without urea; (C) direct mixing in 2.5 x 10(-4) EDTA, pH 8.0; and (D) direct mixing in 0.01 M sodium phosphate, pH 7 [21].

Other interactions of LOC540432

• Molecular cloning of Bac7, a proline- and arginine-rich antimicrobial peptide from bovine neutrophils [22].
• Homologous nucleoplasmic RNA polymerase (EC 2.7.7.6) is a better substrate than arginine-rich histone, phosvitin or casein [23].

Analytical, diagnostic and therapeutic context of LOC540432

• Interactions between arginine-rich histones and deoxyribonucleic acids. II. Circular dichroism [24].
• The arginine-rich histone F3 has been purified by covalent affinity chromatography [25].
• Complexes of DNA with arginine-rich and slightly lysine-rich histones. Transcription and electron microscopy [26].

References