SLBP: Difference between revisions

Jump to navigation Jump to search
m (1 revision imported)
 
(One intermediate revision by one other user not shown)
Line 18: Line 18:
* {{cite journal | vauthors = Choe J, Mi Kim K, Park S, Kyung Lee Y, ((Song O-K)), Kim MK, Lee BG, Song HK, Kim YK | title = Rapid degradation of replication-dependent histone mRNAs largely occurs on mRNAs bound by nuclear cap-binding proteins 80 and 20 | journal = Nucleic Acids Research |  year = 2013 | volume = 41 | issue = 2 | pages = 1307–1318 | doi = 10.1093/nar/gks1196 }}
* {{cite journal | vauthors = Choe J, Mi Kim K, Park S, Kyung Lee Y, ((Song O-K)), Kim MK, Lee BG, Song HK, Kim YK | title = Rapid degradation of replication-dependent histone mRNAs largely occurs on mRNAs bound by nuclear cap-binding proteins 80 and 20 | journal = Nucleic Acids Research |  year = 2013 | volume = 41 | issue = 2 | pages = 1307–1318 | doi = 10.1093/nar/gks1196 }}
* {{cite journal | vauthors = Bansal N, Zhang M, Bhaskar A, Itotia P, Lee E, Shlyakhtenko LS, Lam TT, Fritz A, Berezney R, Lyubchenko YL, Stafford WF, Thapar R | title = Assembly of the SLIP1-SLBP complex on histone mRNA requires heterodimerization and sequential binding of SLBP followed by SLIP1 | journal = Biochemistry |date=January 2013 | volume = 52 | issue = 3 | pages = 520–536 | doi = 10.1021/bi301074r | pmid=23286197 | pmc=3580866}}
* {{cite journal | vauthors = Bansal N, Zhang M, Bhaskar A, Itotia P, Lee E, Shlyakhtenko LS, Lam TT, Fritz A, Berezney R, Lyubchenko YL, Stafford WF, Thapar R | title = Assembly of the SLIP1-SLBP complex on histone mRNA requires heterodimerization and sequential binding of SLBP followed by SLIP1 | journal = Biochemistry |date=January 2013 | volume = 52 | issue = 3 | pages = 520–536 | doi = 10.1021/bi301074r | pmid=23286197 | pmc=3580866}}
* {{cite journal | vauthors = Martin L, Meier M, Lyons SM, Sit RV, Marzluff WF, Quake SR, Chang HY | title = Systematic reconstruction of RNA functional motifs with high-throughput microfluidics | journal = Nature Methods | volume = 9 | issue = 12 | pages = 1192–4 |date=December 2012 | doi = 10.1038/nmeth.2225 }}
* {{cite journal | vauthors = Martin L, Meier M, Lyons SM, Sit RV, Marzluff WF, Quake SR, Chang HY |authorlink7=Howard Y. Chang| title = Systematic reconstruction of RNA functional motifs with high-throughput microfluidics | journal = Nature Methods | volume = 9 | issue = 12 | pages = 1192–4 |date=December 2012 | doi = 10.1038/nmeth.2225 | pmc = 3863600 }}
* {{cite journal | vauthors = Krishnan N, Lam TT, Fritz A, Rempinski D, O'Loughlin K, Minderman H, Berezney R, Marzluff WF, Thapar R | title = The Prolyl Isomerase Pin1 Targets Stem-Loop Binding Protein (SLBP) To Dissociate the SLBP-Histone mRNA Complex Linking Histone mRNA Decay with SLBP Ubiquitination | journal = Mol. Cell. Biol. | volume = 32 | issue = 21 | pages = 4306–22 |date=November 2012 | pmid = 22907757 | doi = 10.1128/MCB.00382-12 }}
* {{cite journal | vauthors = Krishnan N, Lam TT, Fritz A, Rempinski D, O'Loughlin K, Minderman H, Berezney R, Marzluff WF, Thapar R | title = The Prolyl Isomerase Pin1 Targets Stem-Loop Binding Protein (SLBP) To Dissociate the SLBP-Histone mRNA Complex Linking Histone mRNA Decay with SLBP Ubiquitination | journal = Mol. Cell. Biol. | volume = 32 | issue = 21 | pages = 4306–22 |date=November 2012 | pmid = 22907757 | doi = 10.1128/MCB.00382-12 | pmc = 3486140 }}
* {{cite journal | vauthors = Zhang M, Lam TT, Tonelli M, Marzluff WF, Thapar R | title = Interaction of the histone mRNA hairpin with stem-loop binding protein (SLBP) and regulation of the SLBP-RNA complex by phosphorylation and proline isomerization | journal = Biochemistry | volume = 51 | issue = 15 | pages = 3215–31 |date=April 2012 | pmid = 22439849 | doi = 10.1021/bi2018255 }}
* {{cite journal | vauthors = Zhang M, Lam TT, Tonelli M, Marzluff WF, Thapar R | title = Interaction of the histone mRNA hairpin with stem-loop binding protein (SLBP) and regulation of the SLBP-RNA complex by phosphorylation and proline isomerization | journal = Biochemistry | volume = 51 | issue = 15 | pages = 3215–31 |date=April 2012 | pmid = 22439849 | doi = 10.1021/bi2018255 | pmc = 3328597 }}
* {{cite journal | vauthors = Borchers CH, Thapar R, Petrotchenko EV, Torres MP, Speir JP, Easterling M, Dominski Z, Marzluff WF | title = Combined top-down and bottom-up proteomics identifies a phosphorylation site in stem-loop-binding proteins that contributes to high-affinity RNA binding | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 103 | issue = 9 | pages = 3094–9 |date=February 2006 | pmid = 16492733 | pmc = 1413926 | doi = 10.1073/pnas.0511289103 }}
* {{cite journal | vauthors = Borchers CH, Thapar R, Petrotchenko EV, Torres MP, Speir JP, Easterling M, Dominski Z, Marzluff WF | title = Combined top-down and bottom-up proteomics identifies a phosphorylation site in stem-loop-binding proteins that contributes to high-affinity RNA binding | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 103 | issue = 9 | pages = 3094–9 |date=February 2006 | pmid = 16492733 | pmc = 1413926 | doi = 10.1073/pnas.0511289103 }}
* {{cite journal | vauthors = Thapar R, Marzluff WF, Redinbo MR | title = Electrostatic contribution of serine phosphorylation to the Drosophila SLBP--histone mRNA complex | journal = Biochemistry | volume = 43 | issue = 29 | pages = 9401–12 |date=July 2004 | pmid = 15260483 | doi = 10.1021/bi036315j }}
* {{cite journal | vauthors = Thapar R, Marzluff WF, Redinbo MR | title = Electrostatic contribution of serine phosphorylation to the Drosophila SLBP--histone mRNA complex | journal = Biochemistry | volume = 43 | issue = 29 | pages = 9401–12 |date=July 2004 | pmid = 15260483 | doi = 10.1021/bi036315j }}

Latest revision as of 12:00, 10 January 2019

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Histone RNA hairpin-binding protein or stem-loop binding protein (SLBP) is a protein that in humans is encoded by the SLBP gene.[1][2][3]

Species distribution

SLBP has been cloned from humans, C. elegans, D. melanogaster, X. laevis, and sea urchins. The full length human protein has 270 amino acids (31 kDa) with a centrally located RNA binding domain (RBD). The 75 amino acid RBD is well conserved across species, however the remainder of SLBP is highly divergent in most organisms and not homologous to any other protein in the eukaryotic genomes.

Function

This gene encodes a protein that binds to the histone 3' UTR stem-loop structure in replication-dependent histone mRNAs. Histone mRNAs do not contain introns or polyadenylation signals, and are processed by a single endonucleolytic cleavage event downstream of the stem-loop. The stem-loop structure is essential for efficient processing of the histone pre-mRNA but this structure also controls the transport, translation and stability of histone mRNAs. SLBP expression is regulated during S-phase of the cell cycle, increasing more than 10-fold during the latter part of G1.

All SLBP proteins are capable of forming a highly stable complex with histone stem-loop RNA. Complex formation with the histone mRNA stem-loop is achieved by a novel three-helix bundle fold. SLBP proteins also recognize the tetraloop structure of the histone hairpin, the base of the stem, and the 5' flanking region. The crystal structure of human SLBP in complex with the stem-loop RNA as well as the exonuclease Eri1 reveals that the Arg181 residue of SLBP specifically interacts with the second guanine base in the RNA stem.[4] The rest of the protein is intrinsically disordered in fruit-flies as well as in humans. A unique feature of the SLBP RBD is that it is phosphorylated in its RNA binding domain at the Thr171 residue. The SLBP RBD also undergoes proline isomerization about this sequence and is a substrate for the prolyl isomerase Pin1. The N-terminal domain of human SLBP is required for translation activation of histone mRNAs via its interaction with SLIP1. SLBP also interacts with the CBP80 associated protein CTIF to facilitate rapid degradation of histone mRNAs. SLBP is a phosphoprotein and besides T171, it is also phosphorylated at Ser7, Ser20, Ser23, Thr60, Thr61 in mammalian cells. The phosphorylation at Thr60 is mediated by CK2 and Thr61 is by Cyclin A/Cdk1.[3]

References

  1. Martin F, Schaller A, Eglite S, Schumperli D, Muller B (Mar 1997). "The gene for histone RNA hairpin binding protein is located on human chromosome 4 and encodes a novel type of RNA binding protein". EMBO J. 16 (4): 769–78. doi:10.1093/emboj/16.4.769. PMC 1169678. PMID 9049306.
  2. McCombie WR, Martin-Gallardo A, Gocayne JD, FitzGerald M, Dubnick M, Kelley JM, Castilla L, Liu LI, Wallace S, Trapp S (August 1992). "Expressed genes, Alu repeats and polymorphisms in cosmids sequenced from chromosome 4p16.3". Nature Genetics. 1 (5): 348–53. doi:10.1038/ng0892-348. PMID 1338771.
  3. 3.0 3.1 "Entrez Gene: SLBP stem-loop (histone) binding protein".
  4. Dazhi Tan; William F. Marzluff; Zbigniew Dominski; Liang Tong (Jan 2013). "Structure of Histone mRNA Stem-Loop, Human Stem-Loop Binding Protein, and 3′hExo Ternary Complex". Science. 339 (6117): 318–321. doi:10.1126/science.1228705. PMC 3552377. PMID 23329046.

Further reading