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Articles 1 - 3 of 3
Full-Text Articles in Biochemistry, Biophysics, and Structural Biology
Intracellular Lipid-Binding Proteins And Their Genes, David A. Bernlohr, Melanie A. Simpson, Ann Vogel Hertzel, Leonard J. Banaszak
Intracellular Lipid-Binding Proteins And Their Genes, David A. Bernlohr, Melanie A. Simpson, Ann Vogel Hertzel, Leonard J. Banaszak
Department of Biochemistry: Faculty Publications
Intracellular lipid-binding proteins are a family of low-molecularweight single-chain polypeptides that form 1:1 complexes with fatty acids, retinoids, or other hydrophobic ligands. These proteins are products of a large multigene family of unlinked loci distributed throughout the genome. Each lipid-binding protein exhibits a distinctive pattern of tissue distribution. Transcriptional control, regulated by a combination of peroxisome proliferator activated receptors and CCAAT/enhancer-binding proteins, allows for a variety of both cell and tissue-specific expression patterns. In some cells, fatty acids increase the expression of the lipid-binding protein genes. Fatty acids, or their metabolites, are activators of the peroxisome proliferator–activated receptor family of …
Characterization Of Recombinant Soybean Leghemoglobin A And Apolar Distal Histidine Mutants, Mark S. Hargrove, Jennifer K. Barry, Eric Allen Brucker, Michael B. Berry, George N. Phillips, Jr., John S. Olson, Raúl Arredondo-Peter, Jeanenne M. Dean, Robert V. Klucas, Gautam Sarath
Characterization Of Recombinant Soybean Leghemoglobin A And Apolar Distal Histidine Mutants, Mark S. Hargrove, Jennifer K. Barry, Eric Allen Brucker, Michael B. Berry, George N. Phillips, Jr., John S. Olson, Raúl Arredondo-Peter, Jeanenne M. Dean, Robert V. Klucas, Gautam Sarath
Gautam Sarath Publications
The cDNA for soybean leghemoglobin a (Lba) was cloned from a root nodule cDNA library and expressed in Escherichia coli. The crystal structure of the ferric acetate complex of recombinant wild-type Lba was determined at a resolution of 2.2 Å. Rate constants for O2, CO and NO binding to recombinant Lba are identical with those of native soybean Lba. Rate constants for hemin dissociation and auto-oxidation of wild-type Lba were compared with those of sperm whale myoglobin. At 37°C and pH 7, soybean Lba is much less stable than sperm whale myoglobin due both to a fourfold …
Phosphorylation Within The Amino-Terminal Acidic Domain I Of The Phosphoprotein Of Vesicular Stomatitis Virus Is Required For Transcription But Not For Replication, Asit K. Pattnaik, Leroy Hwang, Tong Le, Nathan Englund, Manjula Mathur, Tapas Das, Amiya Banerjee
Phosphorylation Within The Amino-Terminal Acidic Domain I Of The Phosphoprotein Of Vesicular Stomatitis Virus Is Required For Transcription But Not For Replication, Asit K. Pattnaik, Leroy Hwang, Tong Le, Nathan Englund, Manjula Mathur, Tapas Das, Amiya Banerjee
School of Veterinary and Biomedical Sciences: Faculty Publications
Phosphorylation by casein kinase II at three specific residues (S-60, T-62, and S-64) within the acidic domain I of the P protein of Indiana serotype vesicular stomatitis virus has been shown to be critical for in vitro transcription activity of the viral RNA polymerase (P-L) complex. To examine the role of phosphorylation of P protein in transcription as well as replication in vivo, we used a panel of mutant P proteins in which the phosphate acceptor sites in domain I were substituted with alanines or other amino acids. Analyses of the alanine-substituted mutant P proteins for the ability to support …