4tux

drosophila stem-loop binding protein complexed with histone mRNA stem-loopdrosophila stem-loop binding protein complexed with histone mRNA stem-loop

Structural highlights

4tux is a 4 chain structure with sequence from Drosophila melanogaster and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.08Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SLBP_DROME Involved in histone pre-mRNA 3' processing and couples histone mRNA production with the cell cycle. Both maternal and zygotic proteins play an essential and vital function for development.^[1] ^[2]

Publication Abstract from PubMed

Replication-dependent histone mRNAs end with a conserved stem loop that is recognized by stem-loop-binding protein (SLBP). The minimal RNA-processing domain of SLBP is phosphorylated at an internal threonine, and Drosophila SLBP (dSLBP) also is phosphorylated at four serines in its 18-aa C-terminal tail. We show that phosphorylation of dSLBP increases RNA-binding affinity dramatically, and we use structural and biophysical analyses of dSLBP and a crystal structure of human SLBP phosphorylated on the internal threonine to understand the striking improvement in RNA binding. Together these results suggest that, although the C-terminal tail of dSLBP does not contact the RNA, phosphorylation of the tail promotes SLBP conformations competent for RNA binding and thereby appears to reduce the entropic penalty for the association. Increased negative charge in this C-terminal tail balances positively charged residues, allowing a more compact ensemble of structures in the absence of RNA.

Molecular mechanisms for the regulation of histone mRNA stem-loop-binding protein by phosphorylation.,Zhang J, Tan D, DeRose EF, Perera L, Dominski Z, Marzluff WF, Tong L, Hall TM Proc Natl Acad Sci U S A. 2014 Jul 7. pii: 201406381. PMID:25002523^[3]

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

References

↑ Sullivan E, Santiago C, Parker ED, Dominski Z, Yang X, Lanzotti DJ, Ingledue TC, Marzluff WF, Duronio RJ. Drosophila stem loop binding protein coordinates accumulation of mature histone mRNA with cell cycle progression. Genes Dev. 2001 Jan 15;15(2):173-87. PMID:11157774
↑ Sullivan KD, Steiniger M, Marzluff WF. A core complex of CPSF73, CPSF100, and Symplekin may form two different cleavage factors for processing of poly(A) and histone mRNAs. Mol Cell. 2009 May 15;34(3):322-32. doi: 10.1016/j.molcel.2009.04.024. PMID:19450530 doi:10.1016/j.molcel.2009.04.024
↑ Zhang J, Tan D, DeRose EF, Perera L, Dominski Z, Marzluff WF, Tong L, Hall TM. Molecular mechanisms for the regulation of histone mRNA stem-loop-binding protein by phosphorylation. Proc Natl Acad Sci U S A. 2014 Jul 7. pii: 201406381. PMID:25002523 doi:http://dx.doi.org/10.1073/pnas.1406381111

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Sullivan E, Santiago C, Parker ED, Dominski Z, Yang X, Lanzotti DJ, Ingledue TC, Marzluff WF, Duronio RJ. Drosophila stem loop binding protein coordinates accumulation of mature histone mRNA with cell cycle progression. Genes Dev. 2001 Jan 15;15(2):173-87. PMID:11157774

[2] Sullivan KD, Steiniger M, Marzluff WF. A core complex of CPSF73, CPSF100, and Symplekin may form two different cleavage factors for processing of poly(A) and histone mRNAs. Mol Cell. 2009 May 15;34(3):322-32. doi: 10.1016/j.molcel.2009.04.024. PMID:19450530 doi:10.1016/j.molcel.2009.04.024

[3] Zhang J, Tan D, DeRose EF, Perera L, Dominski Z, Marzluff WF, Tong L, Hall TM. Molecular mechanisms for the regulation of histone mRNA stem-loop-binding protein by phosphorylation. Proc Natl Acad Sci U S A. 2014 Jul 7. pii: 201406381. PMID:25002523 doi:http://dx.doi.org/10.1073/pnas.1406381111

[1]

[2]

[3]