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1.
Genome Biol ; 24(1): 45, 2023 03 09.
Artigo em Inglês | MEDLINE | ID: mdl-36894939

RESUMO

Inference and analysis of gene regulatory networks (GRNs) require software that integrates multi-omic data from various sources. The Network Zoo (netZoo; netzoo.github.io) is a collection of open-source methods to infer GRNs, conduct differential network analyses, estimate community structure, and explore the transitions between biological states. The netZoo builds on our ongoing development of network methods, harmonizing the implementations in various computing languages and between methods to allow better integration of these tools into analytical pipelines. We demonstrate the utility using multi-omic data from the Cancer Cell Line Encyclopedia. We will continue to expand the netZoo to incorporate additional methods.


Assuntos
Redes Reguladoras de Genes , Neoplasias , Humanos , Algoritmos , Software , Multiômica , Biologia Computacional/métodos
2.
Bioinformatics ; 36(18): 4765-4773, 2020 09 15.
Artigo em Inglês | MEDLINE | ID: mdl-32860050

RESUMO

MOTIVATION: Conventional methods to analyze genomic data do not make use of the interplay between multiple factors, such as between microRNAs (miRNAs) and the messenger RNA (mRNA) transcripts they regulate, and thereby often fail to identify the cellular processes that are unique to specific tissues. We developed PUMA (PANDA Using MicroRNA Associations), a computational tool that uses message passing to integrate a prior network of miRNA target predictions with target gene co-expression information to model genome-wide gene regulation by miRNAs. We applied PUMA to 38 tissues from the Genotype-Tissue Expression project, integrating RNA-Seq data with two different miRNA target predictions priors, built on predictions from TargetScan and miRanda, respectively. We found that while target predictions obtained from these two different resources are considerably different, PUMA captures similar tissue-specific miRNA-target regulatory interactions in the different network models. Furthermore, the tissue-specific functions of miRNAs we identified based on regulatory profiles (available at: https://kuijjer.shinyapps.io/puma_gtex/) are highly similar between networks modeled on the two target prediction resources. This indicates that PUMA consistently captures important tissue-specific miRNA regulatory processes. In addition, using PUMA we identified miRNAs regulating important tissue-specific processes that, when mutated, may result in disease development in the same tissue. AVAILABILITY AND IMPLEMENTATION: PUMA is available in C++, MATLAB and Python on GitHub (https://github.com/kuijjerlab and https://netzoo.github.io/). SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.


Assuntos
MicroRNAs , Proteínas Reguladoras de Apoptose/genética , Biologia Computacional , Regulação da Expressão Gênica , Redes Reguladoras de Genes , MicroRNAs/genética , RNA Mensageiro , RNA-Seq
3.
Biophys J ; 101(4): 934-42, 2011 Aug 17.
Artigo em Inglês | MEDLINE | ID: mdl-21843485

RESUMO

The photosynthetic light-harvesting systems of purple bacteria and plants both utilize specific carotenoids as quenchers of the harmful (bacterio)chlorophyll triplet states via triplet-triplet energy transfer. Here, we explore how the binding of carotenoids to the different types of light-harvesting proteins found in plants and purple bacteria provides adaptation in this vital photoprotective function. We show that the creation of the carotenoid triplet states in the light-harvesting complexes may occur without detectable conformational changes, in contrast to that found for carotenoids in solution. However, in plant light-harvesting complexes, the triplet wavefunction is shared between the carotenoids and their adjacent chlorophylls. This is not observed for the antenna proteins of purple bacteria, where the triplet is virtually fully located on the carotenoid molecule. These results explain the faster triplet-triplet transfer times in plant light-harvesting complexes. We show that this molecular mechanism, which spreads the location of the triplet wavefunction through the pigments of plant light-harvesting complexes, results in the absence of any detectable chlorophyll triplet in these complexes upon excitation, and we propose that it emerged as a photoprotective adaptation during the evolution of oxygenic photosynthesis.


Assuntos
Complexos de Proteínas Captadores de Luz/química , Luz , Modelos Moleculares , Bacterioclorofilas/química , Carotenoides/química , Carotenoides/metabolismo , Elétrons , Complexos de Proteínas Captadores de Luz/metabolismo , Complexo de Proteína do Fotossistema II/química , Complexo de Proteína do Fotossistema II/metabolismo , Ligação Proteica , Conformação Proteica , Proteobactérias/metabolismo , Espectroscopia de Infravermelho com Transformada de Fourier , Análise Espectral Raman , Spinacia oleracea/metabolismo , Vibração
4.
Biophys J ; 101(4): 1004-13, 2011 Aug 17.
Artigo em Inglês | MEDLINE | ID: mdl-21843493

RESUMO

We report a detailed description of the energy migration dynamics in the phycocyanin 645 (PC645) antenna complex from the photosynthetic alga Chroomonas CCMP270. Many of the cryptophyceae are known to populate greater depths than most other algal families, having developed a 99.5% efficient light-harvesting system. In this study, we used femtosecond time-resolved spectroscopy and global analysis to characterize the excited-state dynamics of PC645. Several different pump colors were selected to excite different fractions of the four phycobiliprotein pairs present in the complex. Measurements were also performed at cryogenic temperature to enhance spectral resolution and selectively promote downhill energy transfers. Upon excitation of the highest-energy bilins (dihydrobiliverdins), energy is transferred from the core of the complex to the periphery within 0.82 ps. Four bilins (mesobiliverdin (MBV) A/B and phycocyanobilins (PCB) 158C/D), which are responsible for the central band of the absorption spectrum, show concerted spectral dynamics. These chromophores show a biphasic decay with lifetimes of 0.6 ps (MBV) and 5-7 ps (PCB 158) to the lowest bilin pair (PCB 82C/D) absorbing around 650-657 nm. Within this lifetime of several picoseconds, the excitations reach the PCB 82 bilins on the two poles at the smaller sides of PC645. A slow 44-46 ps energy transfer step to the lowest-energy PCB 82 bilin concludes the dynamics.


Assuntos
Criptófitas/metabolismo , Transferência de Energia , Complexos de Proteínas Captadores de Luz/metabolismo , Ficocianina/metabolismo , Absorção , Cinética , Análise Espectral , Temperatura
5.
Phys Chem Chem Phys ; 13(38): 17093-103, 2011 Oct 14.
Artigo em Inglês | MEDLINE | ID: mdl-21866281

RESUMO

We further develop the model of energy transfer in the LHCII trimer based on a quantitative fit of the linear spectra (including absorption (OD), linear dichroism (LD), circular dichroism (CD), and fluorescence (FL)) and transient absorption (TA) kinetics upon 650 nm and 662 nm excitation. The spectral shapes and relaxation/migration rates have been calculated using the combined Redfield-Förster approach capable of correctly describing fast relaxation within strongly coupled chlorophyll (Chl) a and b clusters and slow migration between them. Within each monomeric subunit of the trimeric complex there is fast (sub-ps) conversion from Chl's b to Chl's a at the stromal side accompanied by slow (>10 ps) equilibration between the stromal- and lumenal-side Chl a clusters in combination with slow (>13 ps) population of Chl's a from the 'bottleneck' Chl a604 site. The connection between monomeric subunits is determined by exciton coupling between the stromal-side Chl's b from the two adjacent subunits (Chl b601'-608-609 cluster) making a simultaneous fast (sub-ps) population of the Chl's a possible from both subunits. Final equilibration occurs via slow (>20 ps) migration between the Chl a clusters located on different monomeric subunits. This migration includes up-hill transfers from the red-most Chl a610-611-612 clusters located at the peripheral side in each subunit to the Chl a602-603 dimers located at the inner side of the trimeric LHCII complex.


Assuntos
Complexos de Proteínas Captadores de Luz/química , Plantas/química , Proteínas Quinases/química , Transferência de Energia , Cinética , Modelos Moleculares , Multimerização Proteica , Análise Espectral
6.
Biophys J ; 100(11): 2829-38, 2011 Jun 08.
Artigo em Inglês | MEDLINE | ID: mdl-21641329

RESUMO

Plant photosynthesis relies on the capacity of chlorophylls and carotenoids to absorb light. One of the roles of carotenoids is to harvest green-blue light and transfer the excitation energy to the chlorophylls. The corresponding dynamics were investigated here for the first time, to our knowledge, in the CP26 and CP24 minor antenna complexes. The results for the two complexes differ substantially. In CP26 fast transfer (80 fs) occurs from the carotenoid S(2) state to chlorophylls a absorbing at 675 and 678 nm, whereas transfer from the hot S(1) state to the lowest energy chlorophylls is observed in <1 ps. In CP24, energy transfer from the S(2) state leads in 80 fs to the population of chlorophylls b and high-energy chlorophylls a absorbing at 670 nm, whereas the low-energy chlorophylls a are populated only in several picoseconds. The results suggest that CP26 has a structural and functional organization similar to that of LHCII, whereas CP24 differs substantially from the other Lhc complexes, especially regarding the lutein L1 binding domain. No energy transfer from the carotenoid S(1) state to chlorophylls was observed in either complex, suggesting that this state is energetically below the chlorophyll Qy state and therefore may play a role in the quenching of chlorophyll excitations.


Assuntos
Proteínas de Arabidopsis/metabolismo , Carotenoides/metabolismo , Complexos de Proteínas Captadores de Luz/metabolismo , Luz , Complexo de Proteína do Fotossistema II/metabolismo , Absorção , Arabidopsis , Proteínas de Arabidopsis/química , Carotenoides/química , Clorofila/metabolismo , Proteínas de Ligação à Clorofila , Transferência de Energia/efeitos da radiação , Complexos de Proteínas Captadores de Luz/química , Complexo de Proteína do Fotossistema II/química , Ligação Proteica/efeitos da radiação , Análise Espectral
7.
Biophys J ; 99(12): 4056-65, 2010 Dec 15.
Artigo em Inglês | MEDLINE | ID: mdl-21156149

RESUMO

Antenna complexes are key components of plant photosynthesis, the process that converts sunlight, CO2, and water into oxygen and sugars. We report the first (to our knowledge) femtosecond transient absorption study on the light-harvesting pigment-protein complexes CP26 (Lhcb5) and CP24 (Lhcb6) of Photosystem II. The complexes are excited at three different wavelengths in the chlorophyll (Chl) Qy region. Both complexes show a single subpicosecond Chl b to Chl a transfer process. In addition, a reduction in the population of the intermediate states (in the 660-670 nm range) as compared to light-harvesting complex II is correlated in CP26 to the absence of both Chls a604 and b605. However, Chl forms around 670 nm are still present in the Chl a Qy range, which undergoes relaxation with slow rates (10-15 ps). This reduction in intermediate-state amplitude CP24 shows a distinctive narrow band at 670 nm connected with Chls b and decaying to the low-energy Chl a states in 3-5 ps. This 670 nm band, which is fully populated in 0.6 ps together with the Chl a low-energy states, is proposed to originate from Chl 602 or 603. In this study, we monitored the energy flow within two minor complexes, and our results may help elucidate these structures in the future.


Assuntos
Proteínas de Arabidopsis/metabolismo , Arabidopsis/metabolismo , Transferência de Energia , Complexos de Proteínas Captadores de Luz/metabolismo , Complexo de Proteína do Fotossistema II/metabolismo , Proteínas de Ligação à Clorofila , Cinética , Pigmentos Biológicos/metabolismo , Análise Espectral , Fatores de Tempo
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