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Full-Text Articles in Amino Acids, Peptides, and Proteins
Functional Association Between Three Archaeal Aminoacyl-Trna Synthetases, Mette Praetorius-Ibba, Corinne D. Hausmann, Molly Paras, Theresa E. Rogers, Michael Ibba
Functional Association Between Three Archaeal Aminoacyl-Trna Synthetases, Mette Praetorius-Ibba, Corinne D. Hausmann, Molly Paras, Theresa E. Rogers, Michael Ibba
Biology, Chemistry, and Environmental Sciences Faculty Articles and Research
Aminoacyl-tRNA synthetases (aaRSs) are responsible for attaching amino acids to their cognate tRNAs during protein synthesis. In eukaryotes aaRSs are commonly found in multi-enzyme complexes, although the role of these complexes is still not completely clear. Associations between aaRSs have also been reported in archaea, including a complex between prolyl-(ProRS) and leucyl-tRNA synthetases (LeuRS) in Methanothermobacter thermautotrophicus that enhances tRNAPro aminoacylation. Yeast two-hybrid screens suggested that lysyl-tRNA synthetase (LysRS) also associates with LeuRS in M. thermautotrophicus. Co-purification experiments confirmed that LeuRS, LysRS, and ProRS associate in cell-free extracts. LeuRS bound LysRS and ProRS with a comparable KD …
Gene Expression In The Mouse Placenta: Developmental And Stress Responses, Ciprian P. Gheorghe
Gene Expression In The Mouse Placenta: Developmental And Stress Responses, Ciprian P. Gheorghe
Loma Linda University Electronic Theses, Dissertations & Projects
Successful placental development is crucial for optimal growth, maturation, and survival of the embryo/fetus. Placental failure and placental pathology contributes to both morbidity and mortality of the fetus. We sought to understand normal placental development and also placental responses to stress using oligonucleotide microarray technology. To examine genetic aspects of normal placental development, we investigated gene expression patterns in the murine placenta at embryonic day 10.5 (E10.5), E12.5, E15.5, and E17.5. Hypoxia has been identified as a major stressor in placental and fetal development. In order to comprehend more completely hypoxic stress responses we sought to measure gene expression changes …
Aspartyl-Trna Synthetase Is The Target Of Peptidenucleotide Antibiotic Microcin C, Anastasia Metlitskaya, Teymur Kazakov, Aigar Kommer, Olga Pavlova, Mette Praetorius-Ibba, Michael Ibba, Igor Krasheninnkov, Vyacheslav Kolb, Inessa Khmel, Konstantin Severinov
Aspartyl-Trna Synthetase Is The Target Of Peptidenucleotide Antibiotic Microcin C, Anastasia Metlitskaya, Teymur Kazakov, Aigar Kommer, Olga Pavlova, Mette Praetorius-Ibba, Michael Ibba, Igor Krasheninnkov, Vyacheslav Kolb, Inessa Khmel, Konstantin Severinov
Biology, Chemistry, and Environmental Sciences Faculty Articles and Research
Microcin C is a ribosome-synthesized heptapeptide that contains a modified adenosine monophosphate covalently attached to the C-terminal aspartate. Microcin C is a potent inhibitor of bacterial cell growth. Based on the in vivo kinetics of inhibition of macromolecular synthesis, Microcin C targets translation, through a mechanism that remained undefined. Here, we show that Microcin C is a subject of specific degradation inside the sensitive cell. The product of degradation, a modified aspartyl-adenylate containing an N-acylphosphoramidate linkage, strongly inhibits translation by blocking the function of aspartyl-tRNA synthetase.
C To U Editing Stimulates A To I Editing In The Anticodon Loop Of A Cytoplasmic Threonyl Trna In Trypanosoma Brucei, Mary Anne T. Rubio, Frank L. Ragone, Kirk W. Gaston, Michael Ibba, Juan D. Alfonzo
C To U Editing Stimulates A To I Editing In The Anticodon Loop Of A Cytoplasmic Threonyl Trna In Trypanosoma Brucei, Mary Anne T. Rubio, Frank L. Ragone, Kirk W. Gaston, Michael Ibba, Juan D. Alfonzo
Biology, Chemistry, and Environmental Sciences Faculty Articles and Research
Editing of tRNAs is widespread in nature and either changes the decoding properties or restores the folding of a tRNA. Unlike the phylogenetically disperse adenosine (A) to inosine (I) editing, cytosine (C) to uridine (U) editing has only been previously described in organellar tRNAs. We have shown that cytoplasmic tRNAThr(AGU) undergoes two distinct editing events in the anticodon loop: C to U and A to I. In vivo, every inosine-containing tRNAThr is also C to U edited at position 32. In vitro, C to U editing stimulates conversion of A to I at the wobble base. Although …