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Full-Text Articles in Biochemistry
The Rna-Binding Site Of Bacteriophage Qβ Coat Protein, Francis Lim, Marc Spingola, David Peabody
The Rna-Binding Site Of Bacteriophage Qβ Coat Protein, Francis Lim, Marc Spingola, David Peabody
Biology Department Faculty Works
The coat proteins of the RNA bacteriophages Qβ and MS2 are specific RNA binding proteins. Although they possess common tertiary structures, they bind different RNA stem loops and thus provide useful models of specific protein-RNA recognition. Although the RNA-binding site of MS2 coat protein has been extensively characterized previously, little is known about Qβ. Here we describe the isolation of mutants that define the RNA-binding site of Qβ coat protein, showing that, as with MS2, it resides on the surface of a large β-sheet. Mutations are also described that convert Qβ coat protein to the RNA binding specificity of MS2. …
The Rna-Binding Site Of Bacteriophage Qβ Coat Protein, Francis Lim, Marc Spingola, David S. Peabody
The Rna-Binding Site Of Bacteriophage Qβ Coat Protein, Francis Lim, Marc Spingola, David S. Peabody
Marc Spingola
Developmental And Tissue-Specific Expression Of Mouse Pelle-Like Protein Kinase, Marina Trofimova, Amy B. Sprenkle, Melissa Green, Thomas W. Sturgill, Mark G. Goebl, Maureen A. Harrington
Developmental And Tissue-Specific Expression Of Mouse Pelle-Like Protein Kinase, Marina Trofimova, Amy B. Sprenkle, Melissa Green, Thomas W. Sturgill, Mark G. Goebl, Maureen A. Harrington
Amy Sprenkle
Interactions Involving The Human Rna Polymerase Ii Transcription/Nucleotide Excision Repair Complex Tfiih, The Nucleotide Excision Repair Protein Xpg, And Cockayne Syndrome Group B (Csb) Protein, Narayan Iyer, Michael S. Reagan, Kou-Juey Wu, Bertram Canagarajah, Errol C. Friedberg
Interactions Involving The Human Rna Polymerase Ii Transcription/Nucleotide Excision Repair Complex Tfiih, The Nucleotide Excision Repair Protein Xpg, And Cockayne Syndrome Group B (Csb) Protein, Narayan Iyer, Michael S. Reagan, Kou-Juey Wu, Bertram Canagarajah, Errol C. Friedberg
Biology Faculty Publications
The human basal transcription factor TFIIH plays a central role in two distinct processes. TFIIH is an obligatory component of the RNA polymerase II (RNAP II) transcription initiation complex. Additionally, it is believed to be the core structure around which some if not all the components of the nucleotide excision repair (NER) machinery assemble to constitute a nucleotide excision repairosome. At least two of the subunits of TFIIH (XPB and XPD proteins) are implicated in the disease xeroderma pigmentosum (XP). We have exploited the availability of the cloned XPB, XPD, p62, p44, and p34 genes (all …
Use Of The (3)H-Tetracycline Rat Model In The Study Of Skeletal Compartmentalization And Metabolism Of Calcium In The Maturing Male And Female Rat And The Role Of The Skeleton In Calcium Homeostasis In The Adolescent Male Rat, Darrin Lee Demoss
Theses, Dissertations and Capstones
The (3)H-tetracycline bone labeling procedure was employed to monitor bone resorption from urinary loss curves in male and female rats of various ages. In addition, whole body dry skeletal mass and the loss of (3)H-tetracycline from individual bones was determined. It was found that the dry skeletal mass/body mass ratio of 24-week-old females was 30-40% greater than that for males. The urinary loss of (3)H-tetracycline was described by a double exponential equation indicating the presence of two distinct and independent exchangeable bone compartments. Both compartments decrease in size with age, but their label loss activities were different. The label loss …