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The functional study of human proteins using humanized yeast
- Source :
- Journal of Microbiology. 58:343-349
- Publication Year :
- 2020
- Publisher :
- Springer Science and Business Media LLC, 2020.
-
Abstract
- The functional and optimal expression of genes is crucial for survival of all living organisms. Numerous experiments and efforts have been performed to reveal the mechanisms required for the functional and optimal expression of human genes. The yeast Saccharomyces cerevisiae has evolved independently of humans for billions of years. Nevertheless, S. cerevisiae has many conserved genes and expression mechanisms that are similar to those in humans. Yeast is the most commonly used model organism for studying the function and expression mechanisms of human genes because it has a relatively simple genome structure, which is easy to manipulate. Many previous studies have focused on understanding the functions and mechanisms of human proteins using orthologous genes and biological systems of yeast. In this review, we mainly introduce two recent studies that replaced human genes and nucleosomes with those of yeast. Here, we suggest that, although yeast is a relatively small eukaryotic cell, its humanization is useful for the direct study of human proteins. In addition, yeast can be used as a model organism in a broader range of studies, including drug screening.
- Subjects :
- ved/biology.organism_classification_rank.species
Saccharomyces cerevisiae
Computational biology
Applied Microbiology and Biotechnology
Microbiology
03 medical and health sciences
Humans
Nucleosome
Cloning, Molecular
Model organism
Human proteins
Gene
030304 developmental biology
0303 health sciences
biology
030306 microbiology
ved/biology
Proteins
DNA
General Medicine
biology.organism_classification
Yeast
Nucleosomes
Human genome
Microorganisms, Genetically-Modified
Function (biology)
Subjects
Details
- ISSN :
- 19763794 and 12258873
- Volume :
- 58
- Database :
- OpenAIRE
- Journal :
- Journal of Microbiology
- Accession number :
- edsair.doi.dedup.....0d63574fc1fdc936c60fbe6cd1ef1df3