scholarly journals Histone H4 Gene Expression in Shoot Apices Associated with Floral Initiation in Lettuce

2005 ◽  
Vol 74 (2) ◽  
pp. 121-126 ◽  
Author(s):  
O New Lee ◽  
Keisuke Nemoto ◽  
Nobuo Sugiyama
2005 ◽  
Vol 25 (14) ◽  
pp. 6140-6153 ◽  
Author(s):  
Angela Miele ◽  
Corey D. Braastad ◽  
William F. Holmes ◽  
Partha Mitra ◽  
Ricardo Medina ◽  
...  

ABSTRACT Genome replication in eukaryotic cells necessitates the stringent coupling of histone biosynthesis with the onset of DNA replication at the G1/S phase transition. A fundamental question is the mechanism that links the restriction (R) point late in G1 with histone gene expression at the onset of S phase. Here we demonstrate that HiNF-P, a transcriptional regulator of replication-dependent histone H4 genes, interacts directly with p220NPAT, a substrate of cyclin E/CDK2, to coactivate histone genes during S phase. HiNF-P and p220 are targeted to, and colocalize at, subnuclear foci (Cajal bodies) in a cell cycle-dependent manner. Genetic or biochemical disruption of the HiNF-P/p220 interaction compromises histone H4 gene activation at the G1/S phase transition and impedes cell cycle progression. Our results show that HiNF-P and p220 form a critical regulatory module that directly links histone H4 gene expression at the G1/S phase transition to the cyclin E/CDK2 signaling pathway at the R point.


1990 ◽  
Vol 10 (9) ◽  
pp. 4932-4934
Author(s):  
E C Park ◽  
J W Szostak

The N-terminal serine and four conserved lysine residues near the N-terminus of yeast histone H4 are acetylated. We found that a mutation that changed the fourth lysine to alanine resulted in specific derepression of the silent mating type locus HML, while mutations that altered the N-terminal serine or the first three lysines had only minor phenotypic effects. Our results support an active role for histone H4 in the silencing of gene expression at this locus.


1990 ◽  
Vol 10 (9) ◽  
pp. 4932-4934 ◽  
Author(s):  
E C Park ◽  
J W Szostak

The N-terminal serine and four conserved lysine residues near the N-terminus of yeast histone H4 are acetylated. We found that a mutation that changed the fourth lysine to alanine resulted in specific derepression of the silent mating type locus HML, while mutations that altered the N-terminal serine or the first three lysines had only minor phenotypic effects. Our results support an active role for histone H4 in the silencing of gene expression at this locus.


Gene ◽  
2011 ◽  
Vol 483 (1-2) ◽  
pp. 1-10 ◽  
Author(s):  
Li-Jun Liu ◽  
Ronglin Xie ◽  
Sadiq Hussain ◽  
Jane B. Lian ◽  
Jaime Rivera-Perez ◽  
...  

2003 ◽  
Vol 90 (5) ◽  
pp. 387-389 ◽  
Author(s):  
Jude M. Przyborski ◽  
Kathrin Bartels ◽  
Michael Lanzer ◽  
Katherine T. Andrews

1996 ◽  
Vol 10 (3) ◽  
pp. 425-435 ◽  
Author(s):  
Nicole Chaubet ◽  
Martine Flenet ◽  
Bernadette Clement ◽  
Pierre Brignon ◽  
Claude Gigot

2003 ◽  
Vol 23 (2) ◽  
pp. 629-635 ◽  
Author(s):  
John R. Rohde ◽  
Maria E. Cardenas

ABSTRACT The Tor pathway mediates cell growth in response to nutrient availability, in part by inducing ribosomal protein (RP) gene expression via an unknown mechanism. Expression of RP genes coincides with recruitment of the Esa1 histone acetylase to RP gene promoters. We show that inhibition of Tor with rapamycin releases Esa1 from RP gene promoters and leads to histone H4 deacetylation without affecting promoter occupancy by Rap1 and Abf1. Genetic and biochemical evidence identifies Rpd3 as the major histone deacetylase responsible for reversing histone H4 acetylation at RP gene promoters in response to Tor inhibition by rapamycin or nutrient limitation. Our results illustrate that the Tor pathway links nutrient sensing with histone acetylation to control RP gene expression and cell growth.


Sign in / Sign up

Export Citation Format

Share Document