نتایج جستجو برای: nascent polypeptide associated complex alpha
تعداد نتایج: 2378669 فیلتر نتایج به سال:
Microsomes prepared from the rice seed scutellum were incubated in wheat germ extracts (S-100 fraction) to direct the synthesis of alpha-amylase, a secretory protein subject to proteolytic processing (cleavage of the N-terminal signal sequence) as well as glycosylation during its biosynthesis. The characterization and identification of the immunoprecipitable products synthesized were performed ...
گیاهان قادرند در پاسخ به تنش‌های محیطی مکانیسم‌های سازگار خود را فعال کنند و با تغییر در بیان ژن‌هایشان به عوامل محیطی واکنش نشان دهند. لذا در همین راستا از تکنیک پروتئومیکس به منظور شناسایی پروتئین‌های پاسخ‌دهنده به تنش شوری در جو لاین 527 استفاده گردید. برای بررسی اثر تنش شوری طولانی مدت بر روی الگوی پروتئوم جو، بذور لاین 527 (تهیه شده از مؤسسه نهال و بذر) در گلخانه تحقیقاتی گروه زراعت و اصلا...
Bifunctional cross-linking reagents were used to probe the protein environment in the ER membrane of the signal sequence receptor (SSR), a 24-kD integral membrane glycoprotein (Wiedmann, M., T. V. Kurzchalia, E. Hartmann, and T. A. Rapoport. 1987. Nature [Lond.]. 328:830-833). The proximity of several polypeptides was demonstrated. A 22-kD glycoprotein was identified tightly bound to the 34-kD ...
For proteins to enter the secretory pathway, the membrane attachment site (M-site) on ribosomes must bind cotranslationally to the Sec61 complex present in the endoplasmic reticulum membrane. The signal recognition particle (SRP) and its receptor (SR) are required for targeting, and the nascent polypeptide associated complex (NAC) prevents inappropriate targeting of nonsecretory nascent chains....
Proteins with RER-specific signal sequences are cotranslationally translocated across the rough endoplasmic reticulum through a proteinaceous channel composed of oligomers of the Sec61 complex. The Sec61 complex also binds ribosomes with high affinity. The dual function of the Sec61 complex necessitates a mechanism to prevent signal sequence-independent binding of ribosomes to the translocation...
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