scholarly journals Roles for Srp72p in assembly, nuclear export and function of the signal recognition particle

RNA Biology ◽  
2008 ◽  
Vol 5 (2) ◽  
pp. 73-83 ◽  
Author(s):  
Rob W. van Nues ◽  
Eileen Leung ◽  
James C. McDonald ◽  
Iswarya Dantuluru ◽  
Jeremy D. Brown
1990 ◽  
Vol 14 (2-3) ◽  
pp. 71-72 ◽  
Author(s):  
Karin R�misch ◽  
V�ronique Ribes ◽  
Stephen High ◽  
Henrich L�tcke ◽  
David Tollervey ◽  
...  

2004 ◽  
Vol 313 (2) ◽  
pp. 351-355 ◽  
Author(s):  
Christina N. Alavian ◽  
Joan C. Ritland Politz ◽  
Laura B. Lewandowski ◽  
Christine M. Powers ◽  
Thoru Pederson

EMBO Reports ◽  
2001 ◽  
Vol 2 (11) ◽  
pp. 1040-1046 ◽  
Author(s):  
Anat A Herskovits ◽  
Andrei Seluanov ◽  
Ricardo Rajsbaum ◽  
Corinne M ten Hagen‐Jongman ◽  
Tanja Henrichs ◽  
...  

1993 ◽  
Vol 18 (2) ◽  
pp. 143-147 ◽  
Author(s):  
Henrich L�tcke ◽  
Bernhard Dobberstein

2001 ◽  
Vol 153 (4) ◽  
pp. 745-762 ◽  
Author(s):  
Helge Grosshans ◽  
Karina Deinert ◽  
Ed Hurt ◽  
George Simos

The signal recognition particle (SRP) targets nascent secretory proteins to the ER, but how and where the SRP assembles is largely unknown. Here we analyze the biogenesis of yeast SRP, which consists of an RNA molecule (scR1) and six proteins, by localizing all its components. Although scR1 is cytoplasmic in wild-type cells, nuclear localization was observed in cells lacking any one of the four SRP “core proteins” Srp14p, Srp21p, Srp68p, or Srp72p. Consistently, a major nucleolar pool was detected for these proteins. Sec65p, on the other hand, was found in both the nucleoplasm and the nucleolus, whereas Srp54p was predominantly cytoplasmic. Import of the core proteins into the nucleolus requires the ribosomal protein import receptors Pse1p and Kap123p/Yrb4p, which might, thus, constitute a nucleolar import pathway. Nuclear export of scR1 is mediated by the nuclear export signal receptor Xpo1p, is distinct from mRNA transport, and requires, as evidenced by the nucleolar accumulation of scR1 in a dis3/rrp44 exosome component mutant, an intact scR1 3′ end. A subset of nucleoporins, including Nsp1p and Nup159p (Rat7p), are also necessary for efficient translocation of scR1 from the nucleus to the cytoplasm. We propose that assembly of the SRP requires import of all SRP core proteins into the nucleolus, where they assemble into a pre-SRP with scR1. This particle can then be targeted to the nuclear pores and is subsequently exported to the cytoplasm in an Xpo1p-dependent way.


2021 ◽  
Vol 22 (12) ◽  
pp. 6284
Author(s):  
Morgana K. Kellogg ◽  
Sarah C. Miller ◽  
Elena B. Tikhonova ◽  
Andrey L. Karamyshev

Signal recognition particle (SRP) is an RNA and protein complex that exists in all domains of life. It consists of one protein and one noncoding RNA in some bacteria. It is more complex in eukaryotes and consists of six proteins and one noncoding RNA in mammals. In the eukaryotic cytoplasm, SRP co-translationally targets proteins to the endoplasmic reticulum and prevents misfolding and aggregation of the secretory proteins in the cytoplasm. It was demonstrated recently that SRP also possesses an earlier unknown function, the protection of mRNAs of secretory proteins from degradation. In this review, we analyze the progress in studies of SRPs from different organisms, SRP biogenesis, its structure, and function in protein targeting and mRNA protection.


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