Internally transposed signal sequence of carp preproinsulin retains its functions with the signal recognition particle
نویسندگان
چکیده
منابع مشابه
Signal-sequence induced conformational changes in the signal recognition particle
Co-translational protein targeting is an essential, evolutionarily conserved pathway for delivering nascent proteins to the proper cellular membrane. In this pathway, the signal recognition particle (SRP) first recognizes the N-terminal signal sequence of nascent proteins and subsequently interacts with the SRP receptor. For this, signal sequence binding in the SRP54 M domain must be effectivel...
متن کاملImmune-mediated Necrotizing Myopathy With Increased Creatine Phosphokinase and Positive Signal Recognition Particle: A Case Report
Background: Knowledge about Immune-Mediated Necrotizing Myopathy (IMNM) has received significantly attention in recent years. In this study, we report a rare case of IMNM with increased Creatine Phosphokinase (CPK) and positive Signal Recognition Particle (SRP). Clinical Presentation and Intervention: The case was a 67-year-old male patient referred to Firozgar hospital affiliated to the Iran ...
متن کاملThe signal recognition particle.
The signal recognition particle (SRP) and its membrane-associated receptor (SR) catalyze targeting of nascent secretory and membrane proteins to the protein translocation apparatus of the cell. Components of the SRP pathway and salient features of the molecular mechanism of SRP-dependent protein targeting are conserved in all three kingdoms of life. Recent advances in the structure determinatio...
متن کاملInteraction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particle.
The signal-recognition particle (SRP) is a ubiquitous protein-RNA complex that targets proteins to cellular membranes for insertion or secretion. A key player in SRP-mediated protein targeting is the evolutionarily conserved core consisting of the SRP RNA and the multidomain protein SRP54. Communication between the SRP54 domains is critical for SRP function, where signal sequence binding at the...
متن کاملCrystal Structure of the Signal Sequence Binding Subunit of the Signal Recognition Particle
The crystal structure of the signal sequence binding subunit of the signal recognition particle (SRP) from Thermus aquaticus reveals a deep groove bounded by a flexible loop and lined with side chains of conserved hydrophobic residues. The groove defines a flexible, hydrophobic environment that is likely to contribute to the structural plasticity necessary for SRP to bind signal sequences of di...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: FEBS Letters
سال: 1986
ISSN: 0014-5793
DOI: 10.1016/0014-5793(86)80065-5