RESUMO
Continued advancement has forced medical education to accept new ways in which to incorporate technology into its curriculum. As a result, technology has become a cornerstone to all levels of the medical education. This article compiles and discusses various avenues in which technology serves and betters education, ranging from administrative databases to cloud-based storage. Overall, technology can serve various educational purposes, including compilation, circulation, and integration of educational materials. The modalities discussed within this article, while numerous and adaptable, are a small portion of what the technological world has to offer.
Assuntos
Educação de Pós-Graduação em Medicina/métodos , Tecnologia Educacional/métodos , Cirurgia Geral/educação , Coleta de Dados/métodos , Educação a Distância/métodos , Educação a Distância/organização & administração , Educação de Pós-Graduação em Medicina/organização & administração , Tecnologia Educacional/organização & administração , Humanos , Armazenamento e Recuperação da Informação/métodos , América do Norte , Software , Comunicação por VideoconferênciaRESUMO
Post-translational modifications (PTMs) play important roles in regulating a variety of biological processes. To facilitate PTM studies, the genetic code expansion strategy has been utilized to cotranslationally incorporate individual PTMs such as acetylation and phosphorylation into proteins at specific sites. However, recent studies have demonstrated that PTMs actually work together to regulate protein functions and structures. Thus, simultaneous incorporation of multiple distinct PTMs into one protein is highly desirable. In this study, we utilized the genetic incorporation systems of phosphoserine and acetyllysine to install both phosphorylation and acetylation into target proteins simultaneously in Escherichia coli. And we used this system to study the effect of coexisting acetylation and phosphorylation on malate dehydrogenase, demonstrating a practical application of this system in biochemical studies. Furthermore, we tested the mutual orthogonality of three widely used genetic incorporation systems, indicating the possibility of incorporating three distinct PTMs into one protein simultaneously.
Assuntos
Proteínas de Escherichia coli , Escherichia coli , Malato Desidrogenase , Processamento de Proteína Pós-Traducional , Acetilação , Escherichia coli/genética , Escherichia coli/metabolismo , Proteínas de Escherichia coli/biossíntese , Proteínas de Escherichia coli/genética , Malato Desidrogenase/biossíntese , Malato Desidrogenase/genética , Fosforilação/genéticaRESUMO
Protein acetylation plays important roles in many biological processes. Malate dehydrogenase (MDH), a key enzyme in the tricarboxylic acid cycle, has been identified to be acetylated in bacteria by proteomic studies, but no further characterization has been reported. One challenge for studying protein acetylation is to get purely acetylated proteins at specific positions. Here, we applied the genetic code expansion strategy to site-specifically incorporate Nε-acetyllysine into MDH. The acetylation of lysine residues in MDH could enhance its enzyme activity. The Escherichia coli deacetylase CobB could deacetylate acetylated MDH, while the E. coli acetyltransferase YfiQ cannot acetylate MDH efficiently. Our results also demonstrated that acetyl-CoA or acetyl-phosphate could acetylate MDH chemically in vitro. Furthermore, the acetylation level of MDH was shown to be affected by carbon sources in the growth medium.
