Ribosome ER signal xaquence Ass pokpeptidea being muda SRP bindtan ER signial sequence nd caum traralation to paun. SRP binda to an SAP receptor in the ER membrane, which a located nast toa channel. Forthis binding to oce, proteira within SRP wnd the SRP recaptor mut abo be bound by GTP. Cytomal ER membran ER lumen Charnel SRP receptor The GTPbinding proteina wthin SRP nd the SRP recaptor hydralyre their CTP, Caing the relemn of SRP. The lowa trunalation to reauma, and the polypeptide i threded through channal nto the ER lumen FIGURE 17.6 Tarwting of paypeptites lo the endoplamt retkulum mentrae via SRP. Ineukaryoes, ve ral categories of proicins are fiest largeled to the IR membrane via SRP. These include ecreied proleins z well as proleins that are destined to stay in the ER, Golgi apparatus, lysosomes, or vacuoles.

Ribosome ER signal xaquence Ass pokpeptidea being muda SRP bindtan ER signial sequence nd caum traralation to paun. SRP binda to an SAP receptor in the ER membrane, which a located nast toa channel. Forthis binding to oce, proteira within SRP wnd the SRP recaptor mut abo be bound by GTP. Cytomal ER membran ER lumen Charnel SRP receptor The GTPbinding proteina wthin SRP nd the SRP recaptor hydralyre their CTP, Caing the relemn of SRP. The lowa trunalation to reauma, and the polypeptide i threded through channal nto the ER lumen FIGURE 17.6 Tarwting of paypeptites lo the endoplamt retkulum mentrae via SRP. Ineukaryoes, ve ral categories of proicins are fiest largeled to the IR membrane via SRP. These include ecreied proleins z well as proleins that are destined to stay in the ER, Golgi apparatus, lysosomes, or vacuoles.

Biology: The Unity and Diversity of Life (MindTap Course List)

15th Edition

ISBN:9781337408332

Author:Cecie Starr, Ralph Taggart, Christine Evers, Lisa Starr

Publisher:Cecie Starr, Ralph Taggart, Christine Evers, Lisa Starr

Chapter9: From Dna To Protein

Section: Chapter Questions

Problem 1DAA: RIPs as Cancer Drugs Researchers are taking a page from the structure-function relationship of RIPs...

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A plasma membrane ________. a. controls exchanges between the cell and the external environment b. is a mesh of intermediate filaments c. is a type of extracellular matrix
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RIPs as Cancer Drugs Researchers are taking a page from the structure-function relationship of RIPs in their quest for cancer treatments. The most toxic RIPs, remember, have one domain that interferes with ribosomes, and another that carries them into cells. Melissa Cheung and her colleagues incorporated a peptide that binds to skin cancer cells into the enzymatic part of an RIP, the E. coli Shiga-like toxin. The researchers created a new RIP that specifically kills .skin cancer cells, which are notoriously resistant to established therapies. Some of their results are shown in FIGURE 9.17. FIGURE 9.17 Effect of an engineered RIP on cancer cells. The model on the left shows the enzyme portion of E. coli Shiga-like toxin engineered to carry a small sequence of amino acids (in blue) that targets skin cancer cells. (Red indicates the active site.) The graph on the right shows the effect of this engineered RIP on human cancer cells of the skin (); breast () liver (); and prostate (). At what concentration of RIP did all of the different kinds of cells survive?
RIPs as Cancer Drugs Researchers are taking a page from the structure-function relationship of RIPs in their quest for cancer treatments. The most toxic RIPs, remember, have one domain that interferes with ribosomes, and another that carries them into cells. Melissa Cheung and her colleagues incorporated a peptide that binds to skin cancer cells into the enzymatic part of an RIP, the E. coli Shiga-like toxin. The researchers created a new RIP that specifically kills skin cancer cells, which are notoriously resistant to established therapies. Some of their results are shown in FIGURE 9.17. FIGURE 9.17 Effect of an engineered RIP on cancer cells. The model on the left shows the enzyme portion of E. coli Shiga-like toxin engineered to carry a small sequence of amino acids (in blue) that targets skin cancer cells. (Red indicates the active site.) The graph on the right shows the effect of this engineered RIP on human cancer cells of the skin (); breast () liver (); and prostate (). Which cells survived best at 1 microgram per liter RIP?
RIPs as Cancer Drugs Researchers are taking a page from the structure-function relationship of RIPs in their quest for cancer treatments. The most toxic RIPs, remember, have one domain that interferes with ribosomes, and another that carries them into cells. Melissa Cheung and her colleagues incorporated a peptide that binds to skin cancer cells into the enzymatic part of an RIP, the E. coli Shiga-like toxin. The researchers created a new RIP that specifically kills skin cancer cells, which are notoriously resistant to established therapies. Some of their results are shown in FIGURE 9.17. FIGURE 9.17 Effect of an engineered RIP on cancer cells. The model on the left shows the enzyme portion of E. coli Shiga-like toxin engineered to carry a small sequence of amino acids (in blue) that targets skin cancer cells. (Red indicates the active site.) The graph on the right shows the effect of this engineered RIP on human cancer cells of the skin (); breast () liver (); and prostate (). Why are some of the data points linked by curved lines?
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