Hsp70: Difference between revisions
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=='''Overview'''== | =='''Overview'''== | ||
Chaperon proteins function to assist in the folding of newly translated proteins unable to fold on their own and even refold proteins that have become nonfunctional due to some type of misfolding. Misfolding can be caused by several different types of stressors such as high temperature, starvation, inflammation, dehydration, or nitrogen deficiency. Heat shock proteins, primarily the Hsp70 family, partially bind to the protein’s exposed hydrophobic surfaces, to promote protein refolding and prevent interactions that might lead to aggregation <ref>Sharma, D., & Masison, D. (2009). Hsp70 Structure, Function, Regulation and Influence on Yeast Prions. Protein & Peptide Letters, 16(6), 571-581. doi:10.2174/092986609788490230</ref>. | Chaperon proteins function to assist in the folding of newly translated proteins unable to fold on their own and even refold proteins that have become nonfunctional due to some type of misfolding. Misfolding can be caused by several different types of stressors such as high temperature, starvation, inflammation, dehydration, or nitrogen deficiency. Heat shock proteins, primarily the '''Hsp70''' family, partially bind to the protein’s exposed hydrophobic surfaces, to promote protein refolding and prevent interactions that might lead to aggregation <ref>Sharma, D., & Masison, D. (2009). Hsp70 Structure, Function, Regulation and Influence on Yeast Prions. Protein & Peptide Letters, 16(6), 571-581. doi:10.2174/092986609788490230</ref>. | ||
There are 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 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 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 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>. | ||