Cover Image

Structure of the complete bacterial SRP Alu domain

The Alu domain of the signal recognition particle (SRP) arrests protein biosynthesis by competition with elongation factor binding on the ribosome. The mammalian Alu domain is a protein-RNA complex, while prokaryotic Alu domains are protein-free with significant extensions of the RNA. Here we report...

Full description

Saved in:
Bibliographic Details
Main Authors: Kempf, Georg (Author) , Wild, Klemens (Author) , Sinning, Irmgard (Author)
Format: Article (Journal)
Language:English
Published: 30 September 2014
In: Nucleic acids research
Year: 2014, Volume: 42, Issue: 19, Pages: 12284-12294
ISSN:1362-4962
DOI:10.1093/nar/gku883
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1093/nar/gku883
Get full text
Author Notes:Georg Kempf, Klemens Wild and Irmgard Sinning

MARC

LEADER 00000caa a2200000 c 4500
001 1748129554
003 DE-627
005 20230426072717.0
007 cr uuu---uuuuu
008 210211s2014 xx |||||o 00| ||eng c
024 7 |a 10.1093/nar/gku883  |2 doi 
035 |a (DE-627)1748129554 
035 |a (DE-599)KXP1748129554 
035 |a (OCoLC)1341392484 
040 |a DE-627  |b ger  |c DE-627  |e rda 
041 |a eng 
084 |a 30  |2 sdnb 
100 1 |a Kempf, Georg  |e VerfasserIn  |0 (DE-588)1133100201  |0 (DE-627)888264186  |0 (DE-576)48911847X  |4 aut 
245 1 0 |a Structure of the complete bacterial SRP Alu domain  |c Georg Kempf, Klemens Wild and Irmgard Sinning 
264 1 |c 30 September 2014 
300 |a 11 
336 |a Text  |b txt  |2 rdacontent 
337 |a Computermedien  |b c  |2 rdamedia 
338 |a Online-Ressource  |b cr  |2 rdacarrier 
500 |a Gesehen am 11.02.2021 
520 |a The Alu domain of the signal recognition particle (SRP) arrests protein biosynthesis by competition with elongation factor binding on the ribosome. The mammalian Alu domain is a protein-RNA complex, while prokaryotic Alu domains are protein-free with significant extensions of the RNA. Here we report the crystal structure of the complete Alu domain of Bacillus subtilis SRP RNA at 2.5 Å resolution. The bacterial Alu RNA reveals a compact fold, which is stabilized by prokaryote-specific extensions and interactions. In this ‘closed’ conformation, the 5′ and 3′ regions are clamped together by the additional helix 1, the connecting 3-way junction and a novel minor groove interaction, which we term the ‘minor-saddle motif’ (MSM). The 5′ region includes an extended loop-loop pseudoknot made of five consecutive Watson-Crick base pairs. Homology modeling with the human Alu domain in context of the ribosome shows that an additional lobe in the pseudoknot approaches the large subunit, while the absence of protein results in the detachment from the small subunit. Our findings provide the structural basis for purely RNA-driven elongation arrest in prokaryotes, and give insights into the structural adaption of SRP RNA during evolution. 
700 1 |a Wild, Klemens  |e VerfasserIn  |0 (DE-588)1049291190  |0 (DE-627)781602394  |0 (DE-576)177410892  |4 aut 
700 1 |a Sinning, Irmgard  |d 1960-  |e VerfasserIn  |0 (DE-588)1027598617  |0 (DE-627)72945133X  |0 (DE-576)166290580  |4 aut 
773 0 8 |i Enthalten in  |t Nucleic acids research  |d Oxford : Oxford Univ. Press, 1974  |g 42(2014), 19, Seite 12284-12294  |h Online-Ressource  |w (DE-627)26813250X  |w (DE-600)1472175-2  |w (DE-576)07760878X  |x 1362-4962  |7 nnas  |a Structure of the complete bacterial SRP Alu domain 
773 1 8 |g volume:42  |g year:2014  |g number:19  |g pages:12284-12294  |g extent:11  |a Structure of the complete bacterial SRP Alu domain 
856 4 0 |u https://doi.org/10.1093/nar/gku883  |x Verlag  |x Resolving-System  |z lizenzpflichtig  |3 Volltext 
951 |a AR 
992 |a 20210211 
993 |a Article 
994 |a 2014 
998 |g 1027598617  |a Sinning, Irmgard  |m 1027598617:Sinning, Irmgard  |d 700000  |d 711000  |d 120000  |d 140000  |e 700000PS1027598617  |e 711000PS1027598617  |e 120000PS1027598617  |e 140000PS1027598617  |k 0/700000/  |k 1/700000/711000/  |k 0/120000/  |k 0/140000/  |p 3  |y j 
998 |g 1049291190  |a Wild, Klemens  |m 1049291190:Wild, Klemens  |d 700000  |d 711000  |d 120000  |e 700000PW1049291190  |e 711000PW1049291190  |e 120000PW1049291190  |k 0/700000/  |k 1/700000/711000/  |k 0/120000/  |p 2 
998 |g 1133100201  |a Kempf, Georg  |m 1133100201:Kempf, Georg  |d 500000  |d 500638  |e 500000PK1133100201  |e 500638PK1133100201  |k 0/500000/  |k 1/500000/500638/  |p 1  |x j 
999 |a KXP-PPN1748129554  |e 3851524772 
BIB |a Y 
SER |a journal 
JSO |a {"origin":[{"dateIssuedKey":"2014","dateIssuedDisp":"30 September 2014"}],"note":["Gesehen am 11.02.2021"],"physDesc":[{"extent":"11 S."}],"relHost":[{"title":[{"title_sort":"Nucleic acids research","title":"Nucleic acids research"}],"part":{"year":"2014","volume":"42","extent":"11","pages":"12284-12294","text":"42(2014), 19, Seite 12284-12294","issue":"19"},"disp":"Structure of the complete bacterial SRP Alu domainNucleic acids research","type":{"bibl":"periodical","media":"Online-Ressource"},"language":["eng"],"titleAlt":[{"title":"NAR online"},{"title":"NAR"},{"title":"Database issue"},{"title":"Web server issue"}],"note":["Gesehen am 15.09.2025","Ungezählte Beil.: Database issue; Web server issue"],"origin":[{"dateIssuedDisp":"1974-","publisher":"Oxford Univ. Press","publisherPlace":"Oxford","dateIssuedKey":"1974"}],"physDesc":[{"extent":"Online-Ressource"}],"recId":"26813250X","pubHistory":["1.1974 -"],"id":{"zdb":["1472175-2"],"eki":["26813250X"],"issn":["1362-4962"]}}],"person":[{"given":"Georg","family":"Kempf","role":"aut","display":"Kempf, Georg"},{"family":"Wild","given":"Klemens","role":"aut","display":"Wild, Klemens"},{"given":"Irmgard","family":"Sinning","role":"aut","display":"Sinning, Irmgard"}],"title":[{"title":"Structure of the complete bacterial SRP Alu domain","title_sort":"Structure of the complete bacterial SRP Alu domain"}],"recId":"1748129554","type":{"bibl":"article-journal","media":"Online-Ressource"},"name":{"displayForm":["Georg Kempf, Klemens Wild and Irmgard Sinning"]},"language":["eng"],"id":{"doi":["10.1093/nar/gku883"],"eki":["1748129554"]}} 
SRT |a KEMPFGEORGSTRUCTUREO3020 

Similar Items