Hsp70: Difference between revisions
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There are even forms of Hsp70 that are specialized for protein transport into mitochondria and chloroplasts. The proteins transferred into these organelles are not in their mature states yet. Hsp70’s actually bind to the newly translated polypeptides keeping them unfolded until they are in the organelle. Once they are in the designated organelle, their interiors contain specialized Hsp70’s (mitochondrial or chloroplast Hsp70) that fold the polypeptides into a stable, functional state <ref>Plopper, G. (2016). Cytosolic Proteins Targeted to the Mitochondria or Chloroplasts Contain an N-Terminal Signal Sequence. In Principles of Cell Biology (2nd ed.). Burlington, MA: Jones and Bartlett Learning</ref>. | There are even forms of Hsp70 that are specialized for protein transport into mitochondria and chloroplasts. The proteins transferred into these organelles are not in their mature states yet. Hsp70’s actually bind to the newly translated polypeptides keeping them unfolded until they are in the organelle. Once they are in the designated organelle, their interiors contain specialized Hsp70’s (mitochondrial or chloroplast Hsp70) that fold the polypeptides into a stable, functional state <ref>Plopper, G. (2016). Cytosolic Proteins Targeted to the Mitochondria or Chloroplasts Contain an N-Terminal Signal Sequence. In Principles of Cell Biology (2nd ed.). Burlington, MA: Jones and Bartlett Learning</ref>. | ||
Hsp70 function is critical to homeostasis. Protein aggregation is not typically beneficial to most organisms. For example, protein aggregation in different areas of the brain can lead to certain neurodegenerative diseases such as Alzheimer’s and Parkinson’s disease. Hsp70’s promotion of refolding is key to make the misfolded protein functional once again. The many members of the Hsp70 family are highly conserved <ref name="Evans">Evans, C. G., Chang, L., & Gestwicki, J. E. (2010). Heat Shock Protein 70 (Hsp70) as an Emerging Drug Target. Journal of Medicinal Chemistry, 53(12), 4585-4602. doi:10.1021/jm100054f</ref>. This reiterates the fact that these proteins are vital to most organisms. When something is widely expressed and highly conserved it tells us it has been beneficial to cells and organisms for a very long time | Hsp70 function is critical to homeostasis. Protein aggregation is not typically beneficial to most organisms. For example, protein aggregation in different areas of the brain can lead to certain neurodegenerative diseases such as Alzheimer’s and Parkinson’s disease. Hsp70’s promotion of refolding is key to make the misfolded protein functional once again. The many members of the Hsp70 family are highly conserved <ref name="Evans">Evans, C. G., Chang, L., & Gestwicki, J. E. (2010). Heat Shock Protein 70 (Hsp70) as an Emerging Drug Target. Journal of Medicinal Chemistry, 53(12), 4585-4602. doi:10.1021/jm100054f</ref>. This reiterates the fact that these proteins are vital to most organisms. When something is widely expressed and highly conserved it tells us it has been beneficial to cells and organisms for a very long time and there was no need for change. | ||
==''' Structure '''== | ==''' Structure '''== | ||