4l8r

Structure of mrna stem-loop, human stem-loop binding protein and 3'hexo ternary complexStructure of mrna stem-loop, human stem-loop binding protein and 3'hexo ternary complex

Structural highlights

4l8r is a 5 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 4hxh. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ERI1_HUMAN RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs. Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA. Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs.^[1] ^[2]

Publication Abstract from PubMed

Metazoan replication-dependent histone messenger RNAs (mRNAs) have a conserved stem-loop (SL) at their 3'-end. The stem-loop binding protein (SLBP) specifically recognizes the SL to regulate histone mRNA metabolism, and the 3'-5' exonuclease 3'hExo trims its 3'-end after processing. We report the crystal structure of a ternary complex of human SLBP RNA binding domain, human 3'hExo, and a 26-nucleotide SL RNA. Only one base of the SL is recognized specifically by SLBP, and the two proteins primarily recognize the shape of the RNA. SLBP and 3'hExo have no direct contact with each other, and induced structural changes in the loop of the SL mediate their cooperative binding. The 3' flanking sequence is positioned in the 3'hExo active site, but the ternary complex limits the extent of trimming.

Structure of histone mRNA stem-loop, human stem-loop binding protein, and 3'hExo ternary complex.,Tan D, Marzluff WF, Dominski Z, Tong L Science. 2013 Jan 18;339(6117):318-21. doi: 10.1126/science.1228705. PMID:23329046^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Dominski Z, Yang XC, Kaygun H, Dadlez M, Marzluff WF. A 3' exonuclease that specifically interacts with the 3' end of histone mRNA. Mol Cell. 2003 Aug;12(2):295-305. PMID:14536070
↑ Yang XC, Purdy M, Marzluff WF, Dominski Z. Characterization of 3'hExo, a 3' exonuclease specifically interacting with the 3' end of histone mRNA. J Biol Chem. 2006 Oct 13;281(41):30447-54. Epub 2006 Aug 15. PMID:16912046 doi:10.1074/jbc.M602947200
↑ Tan D, Marzluff WF, Dominski Z, Tong L. Structure of histone mRNA stem-loop, human stem-loop binding protein, and 3'hExo ternary complex. Science. 2013 Jan 18;339(6117):318-21. doi: 10.1126/science.1228705. PMID:23329046 doi:10.1126/science.1228705

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OCA

[1] Dominski Z, Yang XC, Kaygun H, Dadlez M, Marzluff WF. A 3' exonuclease that specifically interacts with the 3' end of histone mRNA. Mol Cell. 2003 Aug;12(2):295-305. PMID:14536070

[2] Yang XC, Purdy M, Marzluff WF, Dominski Z. Characterization of 3'hExo, a 3' exonuclease specifically interacting with the 3' end of histone mRNA. J Biol Chem. 2006 Oct 13;281(41):30447-54. Epub 2006 Aug 15. PMID:16912046 doi:10.1074/jbc.M602947200

[3] Tan D, Marzluff WF, Dominski Z, Tong L. Structure of histone mRNA stem-loop, human stem-loop binding protein, and 3'hExo ternary complex. Science. 2013 Jan 18;339(6117):318-21. doi: 10.1126/science.1228705. PMID:23329046 doi:10.1126/science.1228705

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