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Exciting new results from research group led by Ivar Ilves reveals a ๐ต๐ถ๐ด๐ต๐น๐ ๐ฐ๐ผ๐ป๐๐ฒ๐ฟ๐๐ฒ๐ฑ ๐ฝ๐ต๐ผ๐๐ฝ๐ต๐ผ๐ฟ๐๐น๐ฎ๐๐ถ๐ผ๐ป ๐บ๐ฒ๐ฐ๐ต๐ฎ๐ป๐ถ๐๐บ that regulates the interaction between the ๐๐ ๐ ๐ต๐ฒ๐น๐ถ๐ฐ๐ฎ๐๐ฒ and its forked DNA substrate. Our very own QC Manager (GMP and GMP Process Development) Nele Tamberg and Key Account and Technology Officer for our Transient protein production - Lauri Peil were co-authors for the article published in the Journal of Biological Chemistry, their study deepens our understanding of how cells control ๐ด๐ฒ๐ป๐ผ๐บ๐ถ๐ฐ ๐๐ก๐ ๐ฟ๐ฒ๐ฝ๐น๐ถ๐ฐ๐ฎ๐๐ถ๐ผ๐ป, a fundamental process essential for life.
๐น ๐ ๐จ๐ป๐ถ๐๐ฒ๐ฟ๐๐ฎ๐น ๐๐ผ๐ป๐๐ฟ๐ผ๐น ๐ฆ๐๐๐๐ฒ๐บ: The study finds that a phosphorylation site in the MCM3 subunit of CMG is conserved from yeast to humans, suggesting a shared regulatory mechanism across eukaryotes.
๐น ๐๐บ๐ฝ๐น๐ถ๐ฐ๐ฎ๐๐ถ๐ผ๐ป๐ ๐ณ๐ผ๐ฟ ๐๐ฎ๐ป๐ฐ๐ฒ๐ฟ & ๐๐ฒ๐ป๐ฒ๐๐ถ๐ฐ ๐๐ถ๐๐ผ๐ฟ๐ฑ๐ฒ๐ฟ๐: Since errors in DNA replication are linked to cancer and genetic diseases, understanding this regulation could lead to new therapeutic strategies.
๐น ๐ฃ๐ผ๐๐ฒ๐ป๐๐ถ๐ฎ๐น ๐ถ๐ป ๐๐ถ๐ผ๐๐ฒ๐ฐ๐ต๐ป๐ผ๐น๐ผ๐ด๐: The ability to fine-tune DNA replication could be useful in fields like synthetic biology and genomic medicine.
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Discovery of a conserved phosphorylation site in the MCM3 subunit of the CMG helicase.
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Proposed mechanism: Phosphorylation at this site controls how the helicase interacts with DNA, ensuring accurate and efficient replication.
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Potential role in stress response: This modification may help stabilize replication forks during cellular stress.
This research not only deepens our understanding of ๐ต๐ผ๐ ๐๐ก๐ ๐ฟ๐ฒ๐ฝ๐น๐ถ๐ฐ๐ฎ๐๐ถ๐ผ๐ป ๐ถ๐ ๐ฟ๐ฒ๐ด๐๐น๐ฎ๐๐ฒ๐ฑ but also opens doors for future applications in cancer research, biotechnology, and disease modeling.
Kudos to the authors for this outstanding contribution!
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