Transcriptional control of plant storage protein genes

doi:10.1098/rstb.1993.0149

Transcriptional control of plant storage protein genes

Philosophical Transactions of the Royal Society B Biological Sciences ◽

10.1098/rstb.1993.0149 ◽

1993 ◽

Vol 342 (1301) ◽

pp. 209-215 ◽

Cited By ~ 24

Keyword(s):

Gene Expression ◽

Transcriptional Activation ◽

Transcriptional Control ◽

Storage Proteins ◽

Promoter Deletion Analysis ◽

Protein Dna Interactions ◽

Plant Storage

The accumulation of plant storage proteins is controlled primarily by the transcriptional activation of their genes. Two classes of storage proteins, the zygotic or seed-specific, and the somatic, such as tuber proteins, have been studied. Gene expression analysis in transgenic plants has defined small regions of the promoters of such genes that are able to confer the appropriate patterns of expression. Protein-DNA interactions, both in vivo and in vitro , have revealed proteins that bind to regions implicated in expression, and these may be transcription factors. Promoter deletion analysis has determined the role of some of these DNA-binding proteins, such as in determining tissue-specificity or levels of expression. A common theme linking the expression of both classes of storage proteins is the involvement of metabolite levels in directly controlling gene expression.

Download Full-text

Critical Role of the HMGI(Y) Proteins in Adipocytic Cell Growth and Differentiation

Molecular and Cellular Biology ◽

10.1128/mcb.21.7.2485-2495.2001 ◽

2001 ◽

Vol 21 (7) ◽

pp. 2485-2495 ◽

Cited By ~ 52

Author(s):

Rosa Marina Melillo ◽

Giovanna Maria Pierantoni ◽

Stefania Scala ◽

Sabrina Battista ◽

Monica Fedele ◽

...

Keyword(s):

Cell Growth ◽

Transcriptional Activation ◽

Transcriptional Control ◽

Adipogenic Differentiation ◽

Critical Role ◽

Group I ◽

Cell Growth And Differentiation

ABSTRACT The high-mobility group I (HMGI) nonhistone chromosomal proteins HMGI(Y) and HMGI-C have been implicated in defining chromatin structure and in regulating the transcription of several genes. These proteins have been implicated in adipocyte homeostasis: a severe deficiency of fat tissue is found in mice with targeted disruption of the HMGI-C locus, and lipomagenesis in humans is frequently associated with somatic mutations of HMGI genes. The aim of this study was to examine the role of HMGI(Y) proteins in adipocytic cell growth and differentiation. First, we found that differentiation of the preadipocytic 3T3-L1 cell line caused early induction of HMGI(Y) gene expression. Suppression of HMGI(Y) expression by antisense technology dramatically increased the growth rate and impaired adipocytic differentiation in these cells. The process of adipogenic differentiation involves the interplay of several transcription factors, among which is the CCAAT/enhancer-binding protein (C/EBP) family of proteins. These factors are required for the transcriptional activation of adipocyte-specific genes. We also tested the hypothesis that HMGI(Y) might participate in transcriptional control of adipocyte-specific promoters. We found that HMGI(Y) proteins bind C/EBPβ in vivo and in vitro. Furthermore, we show that HMGI(Y) strongly potentiates the capacity of C/EBPβ to transactivate the leptin promoter, an adipose-specific promoter. Taken together, these results indicate that the HMGI(Y) proteins play a critical role in adipocytic cell growth and differentiation.

Download Full-text

Subnuclear compartmentalization of sequence-specific transcription factors and regulation of eukaryotic gene expression

Biochemistry and Cell Biology ◽

10.1139/o05-062 ◽

2005 ◽

Vol 83 (4) ◽

pp. 535-547 ◽

Cited By ~ 7

Author(s):

Gareth N Corry ◽

D Alan Underhill

Keyword(s):

Gene Expression ◽

Transcription Factor ◽

Transcription Factors ◽

Transcriptional Activation ◽

Current Knowledge ◽

Nuclear Architecture ◽

Subnuclear Localization ◽

Modular Structures

To date, the majority of the research regarding eukaryotic transcription factors has focused on characterizing their function primarily through in vitro methods. These studies have revealed that transcription factors are essentially modular structures, containing separate regions that participate in such activities as DNA binding, protein–protein interaction, and transcriptional activation or repression. To fully comprehend the behavior of a given transcription factor, however, these domains must be analyzed in the context of the entire protein, and in certain cases the context of a multiprotein complex. Furthermore, it must be appreciated that transcription factors function in the nucleus, where they must contend with a variety of factors, including the nuclear architecture, chromatin domains, chromosome territories, and cell-cycle-associated processes. Recent examinations of transcription factors in the nucleus have clarified the behavior of these proteins in vivo and have increased our understanding of how gene expression is regulated in eukaryotes. Here, we review the current knowledge regarding sequence-specific transcription factor compartmentalization within the nucleus and discuss its impact on the regulation of such processes as activation or repression of gene expression and interaction with coregulatory factors.Key words: transcription, subnuclear localization, chromatin, gene expression, nuclear architecture.

Download Full-text

GAGA Factor Isoforms Have Distinct but Overlapping Functions In Vivo

Molecular and Cellular Biology ◽

10.1128/mcb.21.24.8565-8574.2001 ◽

2001 ◽

Vol 21 (24) ◽

pp. 8565-8574 ◽

Cited By ~ 20

Author(s):

Anthony J. Greenberg ◽

Paul Schedl

Keyword(s):

Fusion Protein ◽

Transcriptional Activation ◽

Functional Difference ◽

Wild Type ◽

Gaga Factor ◽

Phenotypic Analysis ◽

Alternatively Spliced

ABSTRACT The Drosophila melanogaster GAGA factor (encoded by the Trithorax-like [Trl] gene) is required for correct chromatin architecture at diverse chromosomal sites. The Trl gene encodes two alternatively spliced isoforms of the GAGA factor (GAGA-519 and GAGA-581) that are identical except for the length and sequence of the C-terminal glutamine-rich (Q) domain. In vitro and tissue culture experiments failed to find any functional difference between the two isoforms. We made a set of transgenes that constitutively express cDNAs coding for either of the isoforms with the goal of elucidating their roles in vivo. Phenotypic analysis of the transgenes in Trl mutant background led us to the conclusion that GAGA-519 and GAGA-581 perform different, albeit largely overlapping, functions. We also expressed a fusion protein with LacZ disrupting the Q domain of GAGA-519. This LacZ fusion protein compensated for the loss of wild-type GAGA factor to a surprisingly large extent. This suggests that the Q domain either is not required for the essential functions performed by the GAGA protein or is exclusively used for tetramer formation. These results are inconsistent with a major role of the Q domain in chromatin remodeling or transcriptional activation. We also found that GAGA-LacZ was able to associate with sites not normally occupied by the GAGA factor, pointing to a role of the Q domain in binding site choice in vivo.

Download Full-text

Postrecruitment Function of Yeast Med6 Protein during the Transcriptional Activation by Mediator Complex

Biochemistry Research International ◽

10.1155/2018/6406372 ◽

2018 ◽

Vol 2018 ◽

pp. 1-9

Author(s):

Gwang Sik Kim ◽

Young Chul Lee

Keyword(s):

Gene Expression ◽

Reporter Gene ◽

Transcriptional Activation ◽

Reporter Gene Expression ◽

Temperature Sensitive ◽

Internal Deletion ◽

Cell Extracts ◽

Evolutionarily Conserved

Med6 protein (Med6p) is a hallmark component of evolutionarily conserved Mediator complexes, and the genuine role of Med6p in Mediator functions remains elusive. For the functional analysis ofSaccharomyces cerevisiaeMed6p (scMed6p), we generated a series of scMed6p mutants harboring a small internal deletion. Genetic analysis of these mutants revealed that three regions (amino acids 33–42 (Δ2), 125–134 (Δ5), and 157–166 (Δ6)) of scMed6p are required for cell viability and are located at highly conserved regions of Med6 homologs. Notably, the Med6p-Δ2 mutant was barely detectable in whole-cell extracts and purified Mediator, suggesting a loss of Mediator association and concurrent rapid degradation. Consistent with this, the recombinant forms of Med6p having these mutations partially (Δ2) restore or fail (Δ5 and Δ6) to restore in vitro transcriptional defects caused by temperature-sensitivemed6mutation. In an artificial recruitment assay, Mediator containing a LexA-fused wild-type Med6p or Med6p-Δ5 was recruited to thelexAoperator region with TBP and activated reporter gene expression. However, the recruitment of Mediator containing LexA-Med6p-Δ6 tolexAoperator region resulted in neither TBP recruitment nor reporter gene expression. This result demonstrates a pivotal role of Med6p in the postrecruitment function of Mediator, which is essential for transcriptional activation by Mediator.

Download Full-text

FGF-2–dependent signaling activated in aged human skeletal muscle promotes intramuscular adipogenesis

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.2021013118 ◽

2021 ◽

Vol 118 (37) ◽

pp. e2021013118 ◽

Cited By ~ 1

Author(s):

Sebastian Mathes ◽

Alexandra Fahrner ◽

Umesh Ghoshdastider ◽

Hannes A. Rüdiger ◽

Michael Leunig ◽

...

Keyword(s):

Skeletal Muscle ◽

Transcriptional Activation ◽

Human Skeletal Muscle ◽

Muscle Growth ◽

Muscle Cells ◽

Adeno Associated Virus ◽

Adult Skeletal Muscle

Aged skeletal muscle is markedly affected by fatty muscle infiltration, and strategies to reduce the occurrence of intramuscular adipocytes are urgently needed. Here, we show that fibroblast growth factor-2 (FGF-2) not only stimulates muscle growth but also promotes intramuscular adipogenesis. Using multiple screening assays upstream and downstream of microRNA (miR)-29a signaling, we located the secreted protein and adipogenic inhibitor SPARC to an FGF-2 signaling pathway that is conserved between skeletal muscle cells from mice and humans and that is activated in skeletal muscle of aged mice and humans. FGF-2 induces the miR-29a/SPARC axis through transcriptional activation of FRA-1, which binds and activates an evolutionary conserved AP-1 site element proximal in the miR-29a promoter. Genetic deletions in muscle cells and adeno-associated virus–mediated overexpression of FGF-2 or SPARC in mouse skeletal muscle revealed that this axis regulates differentiation of fibro/adipogenic progenitors in vitro and intramuscular adipose tissue (IMAT) formation in vivo. Skeletal muscle from human donors aged >75 y versus <55 y showed activation of FGF-2–dependent signaling and increased IMAT. Thus, our data highlights a disparate role of FGF-2 in adult skeletal muscle and reveals a pathway to combat fat accumulation in aged human skeletal muscle.

Download Full-text

The Mycobacterium tuberculosis sRNA F6 regulates expression of groEL/S

10.1101/2020.07.15.204107 ◽

2020 ◽

Author(s):

Joanna Houghton ◽

Angela Rodgers ◽

Graham Rose ◽

Kristine B. Arnvig

Keyword(s):

Gene Expression ◽

Mycobacterium Tuberculosis ◽

Small Rnas ◽

Transcriptional Control ◽

Cold Shock ◽

Control Of Gene Expression ◽

Rna Biology ◽

Mouse Model Of Infection

ABSTRACTAlmost 140 years after the identification of Mycobacterium tuberculosis as the etiological agent of tuberculosis, important aspects of its biology remain poorly described. Little is known about the role of post-transcriptional control of gene expression and RNA biology, including the role of most of the small RNAs (sRNAs) identified to date. We have carried out a detailed investigation of the M. tuberculosis sRNA, F6, and show it to be dependent on SigF for expression and significantly induced during in vitro starvation and in a mouse model of infection. However, we found no evidence of attenuation of a ΔF6 strain within the first 20 weeks of infection. A further exploration of F6 using in vitro models of infection suggests a role for F6 as a highly specific regulator of the heat shock repressor, HrcA. Our results point towards a role for F6 during periods of low metabolic activity similar to cold shock and associated with nutrient starvation such as that found in human granulomas in later stages of infection.

Download Full-text

PRMT5 Is Required for Bovine Leukemia Virus Infection In Vivo and Regulates BLV Gene Expression, Syncytium Formation, and Glycosylation In Vitro

Viruses ◽

10.3390/v12060650 ◽

2020 ◽

Vol 12 (6) ◽

pp. 650 ◽

Cited By ~ 1

Author(s):

Wlaa Assi ◽

Tomoya Hirose ◽

Satoshi Wada ◽

Ryosuke Matsuura ◽

Shin-nosuke Takeshima ◽

...

Keyword(s):

Gene Expression ◽

Small Molecule ◽

Bovine Leukemia Virus ◽

Proviral Load ◽

Leukemia Virus ◽

Syncytium Formation ◽

High Proviral Load

Bovine leukemia virus (BLV) is the causative agent of enzootic bovine leukosis, which is the most common neoplastic disease of cattle and is closely related to human T-cell leukemia viruses. We investigated the role of a new host protein, PRMT5, in BLV infection. We found that PRMT5 is overexpressed only in BLV-infected cattle with a high proviral load, but not in those with a low proviral load. Furthermore, this upregulation continued to the lymphoma stage. PRMT5 expression was upregulated in response to experimental BLV infection; moreover, PRMT5 upregulation began in an early stage of BLV infection rather than after a long period of proviral latency. Second, siRNA-mediated PRMT5 knockdown enhanced BLV gene expression at the transcript and protein levels. Additionally, a selective small-molecule inhibitor of PRMT5 (CMP5) enhanced BLV gene expression. Interestingly, CMP5 treatment, but not siRNA knockdown, altered the gp51 glycosylation pattern and increased the molecular weight of gp51, thereby decreasing BLV-induced syncytium formation. This was supported by the observation that CMP5 treatment enhanced the formation of the complex type of N-glycan more than the high mannose type. In conclusion, PRMT5 overexpression is related to the development of BLV infection with a high proviral load and lymphoma stage and PRMT5 inhibition enhances BLV gene expression. This is the first study to investigate the role of PRMT5 in BLV infection in vivo and in vitro and to reveal a novel function for a small-molecule compound in BLV-gp51 glycosylation processing.

Download Full-text

Biologic consequences of androgen receptor (AR) activity in MDV3100-resistant LNCaP cells and dependence on AR full length.

Journal of Clinical Oncology ◽

10.1200/jco.2014.32.4_suppl.74 ◽

2014 ◽

Vol 32 (4_suppl) ◽

pp. 74-74

Author(s):

Yoshiaki Yamamoto ◽

Yohann Loriot ◽

Eliana Beraldi ◽

Tianyuan Zhou ◽

Youngsoo Kim ◽

...

Keyword(s):

Gene Expression ◽

Androgen Receptor ◽

Cell Growth ◽

Functional Role ◽

Full Length ◽

Lncap Cells ◽

Exon 1

74 Background: While recent reports link androgen receptor (AR) variants (AR-Vs) to castration resistant prostate cancer (CRPC), the biological significance of AR-Vs in AR-regulated cell survival and proliferation, independent of AR full length (AR-FL), remains controversial. To define the functional role of AR-FL and AR-Vs in MDV3100-resistant (MDV-R), we designed antisense oligonucleotide (ASO) targeting exon 1 and exon 8 in AR to knockdown AR-FL alone or in combination with AR-Vs and examined these effects in MDV-R LNCaP-derived cells in vitro and in vivo. Methods: We generated by selection MDV-R LNCaP-derived sub-lines that uniformly expressed high levels of both AR-FL and AR-V7 compared to CRPC LNCaP xenografts. Cell growth rates, protein and gene expression were analyzed using crystal violet assay, western blotting and real-time PCR, respectively. Exon 1 and 8 AR-ASO were evaluated in MDV-R49F CRPC LNCaP xenografts. Results: AR-V7 was transiently transfected in MDV-R49F cells and differential knockdown of AR-V7 and/or AR-FL by exon 1 versus exon 8 AR-ASO was used to evaluate relative biologic contributions of AR-FL versus AR-V7 in MDV-R LNCaP AR-V7 overexpressing cells. Exon 1 and 8 AR-ASO treatment in these cells similarly decreased prostate-specific antigen (PSA) expression and induced apoptosis as measured by caspase-3 and PARP cleavage and cell growth inhibition. To further define the functional role of AR-Vs in MDV-R LNCaP cells, we used a CE3 siRNA that specifically silenced AR-V7, but not AR-FL in MDV-R LNCaP cells. AR-V7 knockdown did not decrease PSA levels, did not induce apoptosis, and did not inhibit cell growth. In MDV-R LNCaP cells, exon 1 and 8 ASO similarly suppressed cell growth and AR-regulated gene expression in vitro and in vivo. Conclusions: These results indicate that the AR remains an important driver of MDV3100 resistance and, the biologic consequences mainly driven by AR-FL in MDV-R LNCaP models.

Download Full-text

Yeast Coactivator MBF1 Mediates GCN4-Dependent Transcriptional Activation

Molecular and Cellular Biology ◽

10.1128/mcb.18.9.4971 ◽

1998 ◽

Vol 18 (9) ◽

pp. 4971-4976 ◽

Cited By ~ 70

Author(s):

Ken-ichi Takemaru ◽

Satoshi Harashima ◽

Hitoshi Ueda ◽

Susumu Hirose

Keyword(s):

Gene Expression ◽

Saccharomyces Cerevisiae ◽

Dna Binding ◽

Nuclear Receptor ◽

Transcriptional Activation ◽

Crucial Role ◽

Tata Binding Protein ◽

Binding Region

ABSTRACT Transcriptional coactivators play a crucial role in gene expression by communicating between regulatory factors and the basal transcription machinery. The coactivator multiprotein bridging factor 1 (MBF1) was originally identified as a bridging molecule that connects theDrosophila nuclear receptor FTZ-F1 and TATA-binding protein (TBP). The MBF1 sequence is highly conserved across species fromSaccharomyces cerevisiae to human. Here we provide evidence acquired in vitro and in vivo that yeast MBF1 mediates GCN4-dependent transcriptional activation by bridging the DNA-binding region of GCN4 and TBP. These findings indicate that the coactivator MBF1 functions by recruiting TBP to promoters where DNA-binding regulators are bound.

Download Full-text