scholarly journals Gammaretroviruses tether to mitotic chromatin by directly binding nucleosomal histone proteins

2018 ◽  
Vol 5 (8) ◽  
pp. 385-388 ◽  
Author(s):  
Madushi Wanaguru ◽  
Kate N. Bishop
Keyword(s):  
Histone Proteins ◽  
Nucleosomal Histone ◽  
Mitotic Chromatin

scholarly journals Mitotic post-translational modifications of histones promote chromatin compaction in vitro

Open Biology ◽  
2017 ◽  
Vol 7 (9) ◽  
pp. 170076 ◽  
Author(s):  
Alisa Zhiteneva ◽  
Juan Jose Bonfiglio ◽  
Alexandr Makarov ◽  
Thomas Colby ◽  
Paola Vagnarelli ◽  
...  
Keyword(s):  
Histone Modifications ◽  
Cell Biology ◽  
Transmission Electron Microscopy Analysis ◽  
Histone Proteins ◽  
Post Translational Modifications ◽  
Chromatin Compaction ◽  
Electron Microscopy Analysis ◽  
Core Histones ◽  
Mitotic Chromatin

How eukaryotic chromosomes are compacted during mitosis has been a leading question in cell biology since the nineteenth century. Non-histone proteins such as condensin complexes contribute to chromosome shaping, but appear not to be necessary for mitotic chromatin compaction. Histone modifications are known to affect chromatin structure. As histones undergo major changes in their post-translational modifications during mitotic entry, we speculated that the spectrum of cell-cycle-specific histone modifications might contribute to chromosome compaction during mitosis. To test this hypothesis, we isolated core histones from interphase and mitotic cells and reconstituted chromatin with them. We used mass spectrometry to show that key post-translational modifications remained intact during our isolation procedure. Light, atomic force and transmission electron microscopy analysis showed that chromatin assembled from mitotic histones has a much greater tendency to aggregate than chromatin assembled from interphase histones, even under low magnesium conditions where interphase chromatin remains as separate beads-on-a-string structures. These observations are consistent with the hypothesis that mitotic chromosome formation is a two-stage process with changes in the spectrum of histone post-translational modifications driving mitotic chromatin compaction, while the action of non-histone proteins such as condensin may then shape the condensed chromosomes into their classic mitotic morphology.

scholarly journals Protein lysine crotonylation: past, present, perspective

2021 ◽  
Vol 12 (7) ◽  
Author(s):  
Gaoyue Jiang ◽  
Chunxia Li ◽  
Meng Lu ◽  
Kefeng Lu ◽  
Huihui Li
Keyword(s):  
Cross Talk ◽  
Tissue Injury ◽  
Regulatory Mechanisms ◽  
Biological Processes ◽  
Histone Proteins ◽  
Physiological Functions ◽  
Neuropsychiatric Disease ◽  
Enzymatic Mechanisms ◽  
Substrate Proteins ◽  
Tools And Methods

AbstractLysine crotonylation has been discovered in histone and non-histone proteins and found to be involved in diverse diseases and biological processes, such as neuropsychiatric disease, carcinogenesis, spermatogenesis, tissue injury, and inflammation. The unique carbon–carbon π-bond structure indicates that lysine crotonylation may use distinct regulatory mechanisms from the widely studied other types of lysine acylation. In this review, we discussed the regulation of lysine crotonylation by enzymatic and non-enzymatic mechanisms, the recognition of substrate proteins, the physiological functions of lysine crotonylation and its cross-talk with other types of modification. The tools and methods for prediction and detection of lysine crotonylation were also described.

scholarly journals The Trithorax group protein ASH1 requires a combination of BAH domain and AT hooks, but not the SET domain, for mitotic chromatin binding and survival

Chromosoma ◽  
2021 ◽  
Author(s):  
Philipp A. Steffen ◽  
Christina Altmutter ◽  
Eva Dworschak ◽  
Sini Junttila ◽  
Attila Gyenesei ◽  
...  
Keyword(s):  
Transcriptional Profiling ◽  
Histone H3 ◽  
Chromatin Binding ◽  
Set Domain ◽  
Trithorax Group ◽  
Trxg Protein ◽  
Group Protein ◽  
Bah Domain ◽  
Mitotic Chromatin

AbstractThe Drosophila Trithorax group (TrxG) protein ASH1 remains associated with mitotic chromatin through mechanisms that are poorly understood. ASH1 dimethylates histone H3 at lysine 36 via its SET domain. Here, we identify domains of the TrxG protein ASH1 that are required for mitotic chromatin attachment in living Drosophila. Quantitative live imaging demonstrates that ASH1 requires AT hooks and the BAH domain but not the SET domain for full chromatin binding in metaphase, and that none of these domains are essential for interphase binding. Genetic experiments show that disruptions of the AT hooks and the BAH domain together, but not deletion of the SET domain alone, are lethal. Transcriptional profiling demonstrates that intact ASH1 AT hooks and the BAH domain are required to maintain expression levels of a specific set of genes, including several involved in cell identity and survival. This study identifies in vivo roles for specific ASH1 domains in mitotic binding, gene regulation, and survival that are distinct from its functions as a histone methyltransferase.

scholarly journals Influences of Histone Stoichiometry on the Target Site Preference of Retrotransposons Ty1 and Ty2 in Saccharomyces cerevisiae

Genetics ◽  
1996 ◽  
Vol 142 (3) ◽  
pp. 761-776 ◽  
Author(s):  
Lori A Rinckel ◽  
David J Garfinkel
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Promoter Region ◽  
Target Site ◽  
Site Preference ◽  
Wild Type ◽  
Histone Proteins ◽  
Protein Levels ◽  
In The Wild ◽  
Type Strains ◽  
Orientation Bias

Abstract In Saccharomyces cerevisiae, the target site specificity of the retrotransposon Ty1 appears to involve the Ty integration complex recognizing chromatin structures. To determine whether changes in chromatin structure affect Ty1 and Ty2 target site preference, we analyzed Ty transposition at the CAN1 locus in mutants containing altered levels of histone proteins. A Δhta1-htb1 mutant with decreased levels of H2A and H2B histone proteins showed a pattern of Ty1 and Ty2 insertions at CAN1 that was significantly different from that of both the wild-type and a Δhta2-htb2 mutant, which does not have altered histone protein levels. Altered levels of H2A and H2B proteins disrupted a dramatic orientation bias in the CAN1 promoter region. In the wild-type strains, few Ty1 and Ty2 insertions in the promoter region were oriented opposite to the direction of CAN1 transcription. In the Δhta1-htb1 background, however, numerous Ty1 and Ty2 insertions were in the opposite orientation clustered within the TATA region. This altered insertion pattern does not appear to be due to a bias caused by selecting canavanine resistant isolates in the different HTA1-HTB1 backgrounds. Our results suggest that reduced levels of histone proteins alter Ty target site preference and disrupt an asymmetric Ty insertion pattern.

Synthesis of histone proteins by CPE ligation using a recombinant peptide as the C-terminal building block

2015 ◽  
Vol 158 (5) ◽  
pp. 403-411 ◽  
Author(s):  
Toru Kawakami ◽  
Ryo Yoshikawa ◽  
Yuki Fujiyoshi ◽  
Yuichi Mishima ◽  
Hironobu Hojo ◽  
...  
Keyword(s):  
Building Block ◽  
Histone Proteins ◽  
Recombinant Peptide
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