The U7 snRNP and the hairpin binding protein: Key players in histone mRNA metabolism

1997 ◽  
Vol 8 (6) ◽  
pp. 567-576 ◽  
Author(s):  
Berndt Müller ◽  
Daniel Schümperli
Keyword(s):  
Binding Protein ◽  
Histone Mrna ◽  
Mrna Metabolism ◽  
Key Players ◽  
U7 Snrnp

scholarly journals The stem-loop binding protein regulates translation of histone mRNA during mammalian oogenesis

2005 ◽  
Vol 286 (1) ◽  
pp. 195-206 ◽  
Author(s):  
Patrick Allard ◽  
Qin Yang ◽  
William F. Marzluff ◽  
Hugh J. Clarke
Keyword(s):  
Binding Protein ◽  
Histone Mrna ◽  
Stem Loop

The Saccharomyces cerevisiae poly (A) binding protein (Pab1): Master regulator of mRNA metabolism and cell physiology

Yeast ◽  
2018 ◽  
Vol 36 (1) ◽  
pp. 23-34 ◽  
Author(s):  
Marco Brambilla ◽  
Francesca Martani ◽  
Stefano Bertacchi ◽  
Ilaria Vitangeli ◽  
Paola Branduardi
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Binding Protein ◽  
Cell Physiology ◽  
Master Regulator ◽  
Mrna Metabolism

scholarly journals The RNA-Binding Protein hnRNP K Mediates the Effect of BDNF on Dendritic mRNA Metabolism and Regulates Synaptic NMDA Receptors in Hippocampal Neurons

eNeuro ◽  
2017 ◽  
Vol 4 (6) ◽  
pp. ENEURO.0268-17.2017 ◽  
Author(s):  
Graciano Leal ◽  
Diogo Comprido ◽  
Pasqualino de Luca ◽  
Eduardo Morais ◽  
Luís Rodrigues ◽  
...  
Keyword(s):  
Nmda Receptors ◽  
Hippocampal Neurons ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Hnrnp K ◽  
Mrna Metabolism ◽  
Dendritic Mrna

scholarly journals NMR structure and dynamics of the RNA-binding site for the histone mRNA stem-loop binding protein

RNA ◽  
2002 ◽  
Vol 8 (1) ◽  
pp. 83-96 ◽  
Author(s):  
ERIC S. DEJONG ◽  
WILLIAM F. MARZLUFF ◽  
EDWARD P. NIKONOWICZ
Keyword(s):  
Binding Site ◽  
Rna Binding ◽  
Binding Protein ◽  
Nmr Structure ◽  
Histone Mrna ◽  
Stem Loop ◽  
Structure And Dynamics

scholarly journals The Prolyl Isomerase Pin1 Targets Stem-Loop Binding Protein (SLBP) To Dissociate the SLBP-Histone mRNA Complex Linking Histone mRNA Decay with SLBP Ubiquitination

2012 ◽  
Vol 32 (21) ◽  
pp. 4306-4322 ◽  
Author(s):  
N. Krishnan ◽  
T. T. Lam ◽  
A. Fritz ◽  
D. Rempinski ◽  
K. O'Loughlin ◽  
...  
Keyword(s):  
Mrna Decay ◽  
Binding Protein ◽  
Prolyl Isomerase ◽  
Histone Mrna ◽  
Stem Loop

scholarly journals Concentrating pre-mRNA processing factors in the histone locus body facilitates efficient histone mRNA biogenesis

2016 ◽  
Vol 213 (5) ◽  
pp. 557-570 ◽  
Author(s):  
Deirdre C. Tatomer ◽  
Esteban Terzo ◽  
Kaitlin P. Curry ◽  
Harmony Salzler ◽  
Ivan Sabath ◽  
...  
Keyword(s):  
Messenger Rna ◽  
Mrna Processing ◽  
Histone Mrna ◽  
Histone Mrnas ◽  
Assembly Factor ◽  
U7 Snrnp ◽  
Histone Locus Body ◽  
Histone Locus ◽  
Processing Factors

The histone locus body (HLB) assembles at replication-dependent histone genes and concentrates factors required for histone messenger RNA (mRNA) biosynthesis. FLASH (Flice-associated huge protein) and U7 small nuclear RNP (snRNP) are HLB components that participate in 3′ processing of the nonpolyadenylated histone mRNAs by recruiting the endonuclease CPSF-73 to histone pre-mRNA. Using transgenes to complement a FLASH mutant, we show that distinct domains of FLASH involved in U7 snRNP binding, histone pre-mRNA cleavage, and HLB localization are all required for proper FLASH function in vivo. By genetically manipulating HLB composition using mutations in FLASH, mutations in the HLB assembly factor Mxc, or depletion of the variant histone H2aV, we find that failure to concentrate FLASH and/or U7 snRNP in the HLB impairs histone pre-mRNA processing. This failure results in accumulation of small amounts of polyadenylated histone mRNA and nascent read-through transcripts at the histone locus. Thus, the HLB concentrates FLASH and U7 snRNP, promoting efficient histone mRNA biosynthesis and coupling 3′ end processing with transcription termination.

scholarly journals U7 snRNP is recruited to histone pre-mRNA in a FLASH-dependent manner by two separate regions of the stem–loop binding protein

RNA ◽  
2017 ◽  
Vol 23 (6) ◽  
pp. 938-951 ◽  
Author(s):  
Aleksandra Skrajna ◽  
Xiao-cui Yang ◽  
Katarzyna Bucholc ◽  
Jun Zhang ◽  
Traci M. Tanaka Hall ◽  
...  
Keyword(s):  
Binding Protein ◽  
Dependent Manner ◽  
Stem Loop ◽  
U7 Snrnp

scholarly journals RNA-binding protein Sam68 controls synapse number and local  -actin mRNA metabolism in dendrites

2013 ◽  
Vol 110 (8) ◽  
pp. 3125-3130 ◽  
Author(s):  
M. E. Klein ◽  
T. J. Younts ◽  
P. E. Castillo ◽  
B. A. Jordan
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Mrna Metabolism ◽  
Actin Mrna

scholarly journals Phosphorylation of Stem-Loop Binding Protein (SLBP) on Two Threonines Triggers Degradation of SLBP, the Sole Cell Cycle-Regulated Factor Required for Regulation of Histone mRNA Processing, at the End of S Phase

2003 ◽  
Vol 23 (5) ◽  
pp. 1590-1601 ◽  
Author(s):  
Lianxing Zheng ◽  
Zbigniew Dominski ◽  
Xiao-Cui Yang ◽  
Phillip Elms ◽  
Christy S. Raska ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Amino Acids ◽  
Posttranscriptional Regulation ◽  
Binding Protein ◽  
S Phase ◽  
Mrna Processing ◽  
Histone Mrna ◽  
Stem Loop ◽  
Histone Mrnas ◽  
Nuclear Extracts

ABSTRACT The replication-dependent histone mRNAs, the only eukaryotic mRNAs that do not have poly(A) tails, are present only in S-phase cells. Coordinate posttranscriptional regulation of histone mRNAs is mediated by the stem-loop at the 3′ end of histone mRNAs. The protein that binds the 3′ end of histone mRNA, stem-loop binding protein (SLBP), is required for histone pre-mRNA processing and is involved in multiple aspects of histone mRNA metabolism. SLBP is also regulated during the cell cycle, accumulating as cells enter S phase and being rapidly degraded as cells exit S phase. Mutation of any residues in a TTP sequence (amino acids 60 to 62) or mutation of a consensus cyclin binding site (amino acids 99 to 104) stabilizes SLBP in G2 and mitosis. These two threonines are phosphorylated in late S phase, as determined by mass spectrometry (MS) of purified SLBP from late S-phase cells, triggering SLBP degradation. Cells that express a stable SLBP still degrade histone mRNA at the end of S phase, demonstrating that degradation of SLBP is not required for histone mRNA degradation. Nuclear extracts from G1 and G2 cells are deficient in histone pre-mRNA processing, which is restored by addition of recombinant SLBP, indicating that SLBP is the only cell cycle-regulated factor required for histone pre-mRNA processing.

Sign in / Sign up

Export Citation Format

Share Document