scholarly journals Chromatin Evolution and Molecular Drive in Speciation

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Kyoichi Sawamura
Keyword(s):  
Binding Proteins ◽  
Hybrid Sterility ◽  
Chromatin Binding ◽  
Biological Functions ◽  
Satellite Dnas ◽  
Centromeric Chromatin ◽  
Molecular Drive ◽  
Binding Capability

Are there biological generalities that underlie hybrid sterility or inviability? Recently, around a dozen “speciation genes” have been identified mainly in Drosophila, and the biological functions of these genes are revealing molecular generalities. Major cases of hybrid sterility and inviability seem to result from chromatin evolution and molecular drive in speciation. Repetitive satellite DNAs within heterochromatin, especially at centromeres, evolve rapidly through molecular drive mechanisms (both meiotic and centromeric). Chromatin-binding proteins, therefore, must also evolve rapidly to maintain binding capability. As a result, chromatin binding proteins may not be able to interact with chromosomes from another species in a hybrid, causing hybrid sterility and inviability.

Biological Functions of Latent TGF-β-Binding Proteins and Activation of TGF-β

2008 ◽  
pp. 57-75
Author(s):  
Marko Hyytiäinen ◽  
Katri Koli ◽  
Jorma Keski-Oja
Keyword(s):  
Binding Proteins ◽  
Biological Functions

scholarly journals Identification and characterization of a new isoform of small GTPase RhoE

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Yuan Dai ◽  
Weijia Luo ◽  
Xiaojing Yue ◽  
Wencai Ma ◽  
Jing Wang ◽  
...  
Keyword(s):  
Rho Gtpase ◽  
Small Gtpases ◽  
Small Gtpase ◽  
Biological Functions ◽  
Coding Region ◽  
Alternative Translation ◽  
Rho Family ◽  
Binding Capability ◽  
Identification And Characterization

Abstract The Rho family of GTPases consists of 20 members including RhoE. Here, we discover the existence of a short isoform of RhoE designated as RhoEα, the first Rho GTPase isoform generated from alternative translation. Translation of this new isoform is initiated from an alternative start site downstream of and in-frame with the coding region of the canonical RhoE. RhoEα exhibits a similar subcellular distribution while its protein stability is higher than RhoE. RhoEα contains binding capability to RhoE effectors ROCK1, p190RhoGAP and Syx. The distinct transcriptomes of cells with the expression of RhoE and RhoEα, respectively, are demonstrated. The data propose distinctive and overlapping biological functions of RhoEα compared to RhoE. In conclusion, this study reveals a new Rho GTPase isoform generated from alternative translation. The discovery provides a new scope of understanding the versatile functions of small GTPases and underlines the complexity and diverse roles of small GTPases.

scholarly journals Biological functions and prognostic value of RNA Binding Proteins in clear cell Renal Cell Carcinoma

2020 ◽  
Vol 11 (22) ◽  
pp. 6591-6600 ◽  
Author(s):  
Zhenpeng Zhu ◽  
Anbang He ◽  
Lanruo Lin ◽  
Chunru Xu ◽  
Tianyu Cai ◽  
...  
Keyword(s):  
Renal Cell Carcinoma ◽  
Cell Carcinoma ◽  
Renal Cell ◽  
Prognostic Value ◽  
Binding Proteins ◽  
Rna Binding ◽  
Clear Cell ◽  
Rna Binding Proteins ◽  
Biological Functions ◽  
Cell Renal Cell Carcinoma

Isolation of copper-binding proteins from activated sludge culture

2001 ◽  
Vol 44 (2-3) ◽  
pp. 453-459 ◽  
Author(s):  
K. Fukushi ◽  
S. Kato ◽  
T. Antsuki ◽  
T. Omura
Keyword(s):  
Molecular Weight ◽  
Activated Sludge ◽  
Metal Uptake ◽  
Binding Proteins ◽  
Growth Media ◽  
Copper Binding ◽  
Molecular Weights ◽  
Binding Capability ◽  
Copper Binding Proteins

Six copper-binding microbial proteins were isolated from activated sludge cultures grown on media containing copper at various concentrations. Molecular weights among isolated proteins were ranged from 1.3k to 174k dalton. Isolated proteins were compared for their copper binding capabilities. Proteins isolated from cultures grown in the presence of copper in the growth media exhibited higher copper binding capabilities than those isolated from the culture grown in the absence of copper. The highest metal uptake of 61.23 (mol copper/mol protein) was observed by a protein isolated from a culture grown with copper at a concentration of 0.25 mM. This isolated protein (CBP2) had a molecular weight of 24k dalton. Other protein exhibited copper binding capability of 4.8-32.5 (mol copper/mol protein).

scholarly journals A proteomics approach for the identification of nucleophosmin and heterogeneous nuclear ribonucleoprotein C1/C2 as chromatin-binding proteins in response to DNA double-strand breaks

2005 ◽  
Vol 388 (1) ◽  
pp. 7-15 ◽  
Author(s):  
Seung Yun LEE ◽  
Ji-Hye PARK ◽  
Sungsu KIM ◽  
Eun-Jung PARK ◽  
Yungdae YUN ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Repair ◽  
Binding Proteins ◽  
Double Strand Breaks ◽  
Nuclear Proteins ◽  
Chromatin Binding ◽  
Strand Breaks ◽  
Heterogeneous Nuclear Ribonucleoprotein ◽  
Proteomics Approach ◽  
Nuclear Ribonucleoprotein

Double-strand breaks (DSBs) of chromosomal DNA trigger the cellular response that activates the pathways for DNA repair and cell-cycle checkpoints, and sometimes the pathways leading to cell death if the damage is too severe to be tolerated. Evidence indicates that, upon generation of DNA DSBs, many nuclear proteins that are involved in DNA repair and checkpoints are recruited to chromatin around the DNA lesions. In the present study we used a proteomics approach to identify DNA-damage-induced chromatin-binding proteins in a systematic way. Two-dimensional gel analysis for protein extracts of chromatin from DNA-damage-induced and control HeLa cells identified four proteins as the candidates for DNA-damage-induced chromatin-binding proteins. MALDI–TOF (matrix-assisted laser-desorption ionization–time-of-flight) MS analysis identified these proteins to be NPM (nucleophosmin), hnRNP (heterogeneous nuclear ribonucleoprotein) C1, hnRNP C2 and 37-kDa laminin-receptor precursor, and the identity of these proteins was further confirmed by immunoblot analysis with specific antibodies. We then demonstrated with chromatin-binding assays that NPM and hnRNP C1/C2, the abundant nuclear proteins with pleiotropic functions, indeed bind to chromatin in a DNA-damage-dependent manner, implicating these proteins in DNA repair and/or damage response. Immunofluorescence experiments showed that NPM, normally present in the nucleoli, is mobilized into the nucleoplasm after DNA damage, and that neither NPM nor hnRNP C1/C2 is actively recruited to the sites of DNA breaks. These results suggest that NPM and hnRNP C1/C2 may function at the levels of the global context of chromatin, rather than by specifically targeting the broken DNA.

The role of chromatin conformations in diffusional transport of chromatin-binding proteins: Cartesian lattice simulations

2008 ◽  
Vol 128 (15) ◽  
pp. 155101 ◽  
Author(s):  
Annika Wedemeier ◽  
Ting Zhang ◽  
Holger Merlitz ◽  
Chen-Xu Wu ◽  
Jörg Langowski
Keyword(s):  
Binding Proteins ◽  
Chromatin Binding

scholarly journals The dynamics of HMG protein–chromatin interactions in living cellsThis paper is one of a selection of papers published in this Special Issue, entitled CSBMCB’s 51st Annual Meeting – Epigenetics and Chromatin Dynamics, and has undergone the Journal’s usual peer review process.

2009 ◽  
Vol 87 (1) ◽  
pp. 127-137 ◽  
Author(s):  
Gabi Gerlitz ◽  
Robert Hock ◽  
Tetsuya Ueda ◽  
Michael Bustin
Keyword(s):  
Binding Sites ◽  
Binding Proteins ◽  
Peer Review Process ◽  
High Mobility ◽  
Structural Features ◽  
Chromatin Binding ◽  
Hmg Proteins ◽  
Chromatin Dynamics ◽  
Chromatin Interactions ◽  
Major Factors

The dynamic interaction between nuclear proteins and chromatin leads to the functional plasticity necessary to mount adequate responses to regulatory signals. Here, we review the factors regulating the chromatin interactions of the high mobility group proteins (HMGs), an abundant and ubiquitous superfamily of chromatin-binding proteins in living cells. HMGs are highly mobile and interact with the chromatin fiber in a highly dynamic fashion, as part of a protein network. The major factors that affect the binding of HMGs to chromatin are operative at the level of the single nucleosome. These factors include structural features of the HMGs, competition with other chromatin-binding proteins for nucleosome binding sites, complex formation with protein partners, and post-translational modifications in the protein or in the chromatin-binding sites. The versatile modulation of the interaction between HMG proteins and chromatin plays a role in processes that establish the cellular phenotype.

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