Literature DB >> 15718142

The signal recognition particle and its interactions during protein targeting.

Mario Halic1, Roland Beckmann.   

Abstract

The synthesis of secretory or integral membrane proteins can be directly coupled to their translocation across or insertion into membranes. In co-translational targeting, the translation machine, the ribosome, is transferred to the respective membrane by the signal recognition particle (SRP) and its receptor (SR) as soon as a signal sequence emerges. Protein synthesis can continue at the membrane, with the nascent peptide chain directly inserting into the ribosome-bound protein-conducting channel, the Sec61 complex. During the past two years, several structures have been solved by crystallography and cryo-electron microscopy that represent distinct functional states of the SRP cycle. On this basis, the first structure-based models can be suggested that explain important aspects of protein targeting, such as the SRP-ribosome and SRP-SR interactions.

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Year:  2005        PMID: 15718142     DOI: 10.1016/j.sbi.2005.01.013

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  50 in total

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Review 6.  Three-way RNA junctions with remote tertiary contacts: a recurrent and highly versatile fold.

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9.  Identification of amino acid residues in protein SRP72 required for binding to a kinked 5e motif of the human signal recognition particle RNA.

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10.  Blocking variant surface glycoprotein synthesis in Trypanosoma brucei triggers a general arrest in translation initiation.

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