scholarly journals RPL39L is an example of a recently evolved ribosomal protein paralog that shows highly specific tissue expression patterns and is upregulated in ESCs and HCC tumors

RNA Biology ◽  
2013 ◽  
Vol 11 (1) ◽  
pp. 33-41 ◽  
Author(s):  
Queenie Wing-Lei Wong ◽  
Jia Li ◽  
Sheng Rong Ng ◽  
Seng Gee Lim ◽  
Henry Yang ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Expression Patterns ◽  
Tissue Expression ◽  
Specific Tissue

Cloning and mapping of human PKIB and PKIG, and comparison of tissue expression patterns of three members of the protein kinase inhibitor family, including PKIA

2000 ◽  
Vol 349 (2) ◽  
pp. 403-407 ◽  
Author(s):  
Lihua ZHENG ◽  
Long YU ◽  
Qiang TU ◽  
Min ZHANG ◽  
Hua HE ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Nuclear Export ◽  
Kinase Inhibitor ◽  
Expression Patterns ◽  
Nuclear Export Signal ◽  
Tissue Expression ◽  
Protein Kinase Inhibitor ◽  
The Other ◽  
Dependent Protein

Two novel members of the human cAMP-dependent protein kinase inhibitor (PKI) gene family, PKIB and PKIG, were cloned. The deduced proteins showed 70% and 90% identity with mouse PKIβ and PKIγ respectively. Both the already identified pseudosubstrate site and leucine-rich nuclear export signal motifs were defined from the 11 PKIs of different species. The PKIB and PKIG genes were mapped respectively to chromosome 6q21-22.1, using a radiation hybrid GB4 panel, and to chromosome 20q13.12-13.13, using a Stanford G3 panel. Northern-blot analysis of three PKI isoforms, including the PKIA identified previously, revealed significant differences in their expression patterns. PKIB had two transcripts of 1.9 kb and 1.4 kb. The former transcript was abundant in both placenta and brain and the latter was expressed most abundantly in placenta, highly in brain, heart, liver, pancreas, moderately in kidney, skeletal muscle and colon, and very little in the other eight tissues tested. PKIG was widely expressed as a 1.5-kb transcript with the highest level in heart, hardly detectable in thymus and peripheral blood leucocytes and was moderately expressed in the other tissues, with slightly different levels. However, PKIA was specifically expressed as two transcripts of 3.3 kb and 1.5 kb in heart and skeletal muscle. The distinct expression patterns of the three PKIs suggest that their roles in various tissues are probably different.

scholarly journals Protein structure-based gene expression signatures

2020 ◽  
Author(s):  
R. Rahman ◽  
Y. Xiong ◽  
J. G. C. van Hasselt ◽  
J. Hansen ◽  
E. A. Sobie ◽  
...  
Keyword(s):  
Gene Expression ◽  
Protein Structure ◽  
Mrna Expression ◽  
Expression Patterns ◽  
Drug Effects ◽  
Tissue Expression ◽  
Structural Features ◽  
Biological Phenomena ◽  
Gene Expression Signatures ◽  
Cellular Phenotypes

AbstractGene expression signatures (GES) connect phenotypes to mRNA expression patterns, providing a powerful approach to define cellular identity, function, and the effects of perturbations. However, the use of GES has suffered from vague assessment criteria and limited reproducibility. The structure of proteins defines the functional capability of genes, and hence, we hypothesized that enrichment of structural features could be a generalizable representation of gene sets. We derive structural gene expression signatures (sGES) using features from various levels of protein structure (e.g. domain, fold) encoded by the transcribed genes in GES, to describe cellular phenotypes. Comprehensive analyses of data from the Genotype-Tissue Expression Project (GTEx), ARCHS4, and mRNA expression of drug effects on cardiomyocytes show that structural GES (sGES) are useful for identifying robust signatures of biological phenomena. sGES also enables the characterization of signatures across experimental platforms, facilitates the interoperability of expression datasets, and can describe drug action on cells.

scholarly journals Characterization of the Soybean GmIREG Family Genes and the Function of GmIREG3 in Conferring Tolerance to Aluminum Stress

2020 ◽  
Vol 21 (2) ◽  
pp. 497
Author(s):  
Zhandong Cai ◽  
Peiqi Xian ◽  
Rongbin Lin ◽  
Yanbo Cheng ◽  
Tengxiang Lian ◽  
...  
Keyword(s):  
Transgenic Arabidopsis ◽  
Relative Elongation ◽  
Expression Patterns ◽  
Tissue Expression ◽  
Metal Stress ◽  
Aluminum Stress ◽  
Systematic Analysis ◽  
Aluminum Resistance ◽  
Encoding Genes

The IREG (IRON REGULATED/ferroportin) family of genes plays vital roles in regulating the homeostasis of iron and conferring metal stress. This study aims to identify soybean IREG family genes and characterize the function of GmIREG3 in conferring tolerance to aluminum stress. Bioinformatics and expression analyses were conducted to identify six soybean IREG family genes. One GmIREG, whose expression was significantly enhanced by aluminum stress, GmIREG3, was studied in more detail to determine its possible role in conferring tolerance to such stress. In total, six potential IREG-encoding genes with the domain of Ferroportin1 (PF06963) were characterized in the soybean genome. Analysis of the GmIREG3 root tissue expression patterns, subcellular localizations, and root relative elongation and aluminum content of transgenic Arabidopsis overexpressing GmIREG3 demonstrated that GmIREG3 is a tonoplast localization protein that increases transgenic Arabidopsis aluminum resistance but does not alter tolerance to Co and Ni. The systematic analysis of the GmIREG gene family reported herein provides valuable information for further studies on the biological roles of GmIREGs in conferring tolerance to metal stress. GmIREG3 contributes to aluminum resistance and plays a role similar to that of FeIREG3. The functions of other GmIREG genes need to be further clarified in terms of whether they confer tolerance to metal stress or other biological functions.

New functional aspects of the neuroendocrine marker secretagogin based on the characterization of its rat homolog

2007 ◽  
Vol 293 (1) ◽  
pp. E347-E354 ◽  
Author(s):  
W. Gartner ◽  
G. Vila ◽  
T. Daneva ◽  
A. Nabokikh ◽  
F. Koc-Saral ◽  
...  
Keyword(s):  
Sequence Homology ◽  
Expression Patterns ◽  
Tissue Expression ◽  
Comparative Sequence Analysis ◽  
Cell Fractionation ◽  
Dexamethasone Treatment ◽  
Insulin Synthesis ◽  
Fractionation Analysis ◽  
Insulin Secreting Cells

Secretagogin is a recently cloned human β-cell-expressed EF-hand Ca2+-binding protein. Converging evidence indicates that it exerts Ca2+sensor activity and is involved in regulation of insulin synthesis and secretion. To obtain a potent tool for the extension of its functional analysis in rat in vitro systems, we cloned the rat homolog of human secretagogin. Using comparative sequence analysis, immunostaining, and immunoblotting, we demonstrated a high degree of sequence homology and similar tissue expression patterns of human and rat secretagogin. Highest rat secretagogin expression levels were found in pancreatic β-cells. On the basis of newly generated anti-rat secretagogin antibodies, we established a rat secretagogin-specific sandwich capture ELISA and demonstrated release of secretagogin from viable Rin-5F cells. Dexamethasone treatment of Rin-5F cells resulted in an increased secretagogin release rate, which was inversely correlated with insulin secretion. In contrast, the secretagogin transcription rate was markedly reduced. This resulted in a decreased intracellular secretagogin content under the influence of dexamethasone. Sucrose gradient cell fractionation analysis of Rin-5F cells confirmed the predominant cytosolic localization of secretagogin, with only limited association of secretagogin with insulin granules. The loss of intracellular secretagogin after dexamethasone treatment affected predominantly the insulin granule-associated secretagogin fractions. The sequence homology and the comparable tissue expression patterns of human and rat secretagogin indicate conserved intracellular functions. The effects of dexamethasone on the total secretagogin content in Rin-5F cells and on its intracellular distribution might result in an impaired Ca2+sensitivity of dexamethasone-treated insulin-secreting cells.

Identification and expression analysis of chloroplast ribonucleoproteins (cpRNPs) in Arabidopsis and rice

Genome ◽  
2020 ◽  
Author(s):  
Jiawen Wu ◽  
Huimin Liu ◽  
Shan Lu ◽  
Jian Hua ◽  
Baohong Zou
Keyword(s):  
Expression Analysis ◽  
Stress Responses ◽  
Expression Patterns ◽  
Tissue Expression ◽  
Stability Control ◽  
Rna Recognition Motif ◽  
Chloroplast Targeting ◽  
Genome Wide ◽  
A Genome ◽  
Targeting Signal

Chloroplast ribonucleoproteins (cpRNPs) are implicated in splicing, editing and stability control of chloroplast RNAs as well as in regulating development and stress tolerance. To facilitate a comprehensive understanding of their functions, we carried out a genome-wide identification, curation, and phylogenetic analysis of cpRNP genes in Oryza sativa (rice) and Arabidopsis thaliana (Arabidopsis). Ten cpRNP genes were identified in each of Arabidopsis and rice genomes based on the presence of two RRM (RNA recognition motif) domains and an N-terminal chloroplast targeting signal peptide in the predicted proteins. These proteins are localized to chloroplasts. Gene expression analysis revealed that cpRNPs have differential tissue expression patterns and some cpRNPs are induced by abiotic stresses such as cold, heat and drought. Taken together, our study provides a comprehensive annotation of the cpRNP gene family and their expression patterns in Arabidopsis and rice which will facilitate further studies on their roles in plant growth and stress responses.

scholarly journals Analysis of Gal4 Expression Patterns in Adult Drosophila Females

2020 ◽  
Vol 10 (11) ◽  
pp. 4147-4158
Author(s):  
Lesley N. Weaver ◽  
Tianlu Ma ◽  
Daniela Drummond-Barbosa
Keyword(s):  
Genetic Manipulation ◽  
Expression Patterns ◽  
Cell Types ◽  
Tissue Expression ◽  
Whole Body ◽  
Specific Gene ◽  
Specific Cell ◽  
Gene Pathway ◽  
Gal4 Expression ◽  
Adult Drosophila

Precise genetic manipulation of specific cell types or tissues to pinpoint gene function requirement is a critical step in studies aimed at unraveling the intricacies of organismal physiology. Drosophila researchers heavily rely on the UAS/Gal4/Gal80 system for tissue-specific manipulations; however, it is often unclear whether the reported Gal4 expression patterns are indeed specific to the tissue of interest such that experimental results are not confounded by secondary sites of Gal4 expression. Here, we surveyed the expression patterns of commonly used Gal4 drivers in adult Drosophila female tissues under optimal conditions and found that multiple drivers have unreported secondary sites of expression beyond their published cell type/tissue expression pattern. These results underscore the importance of thoroughly characterizing Gal4 tools as part of a rigorous experimental design that avoids potential misinterpretation of results as we strive for understanding how the function of a specific gene/pathway in one tissue contributes to whole-body physiology.

scholarly journals Tissue- and paralogue-specific functions of acyl-CoA-binding proteins in lipid metabolism in Caenorhabditis elegans

2011 ◽  
Vol 437 (2) ◽  
pp. 231-241 ◽  
Author(s):  
Ida C. Elle ◽  
Karina T. Simonsen ◽  
Louise C. B. Olsen ◽  
Pernille K. Birck ◽  
Sidse Ehmsen ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Unsaturated Fatty Acids ◽  
Expression Patterns ◽  
High Specificity ◽  
Tissue Expression ◽  
Yeast Cells ◽  
Loss Of Function ◽  
C Elegans ◽  
Eukaryotic Species ◽  
Quadruple Mutant

ACBP (acyl-CoA-binding protein) is a small primarily cytosolic protein that binds acyl-CoA esters with high specificity and affinity. ACBP has been identified in all eukaryotic species, indicating that it performs a basal cellular function. However, differential tissue expression and the existence of several ACBP paralogues in many eukaryotic species indicate that these proteins serve distinct functions. The nematode Caenorhabditis elegans expresses seven ACBPs: four basal forms and three ACBP domain proteins. We find that each of these paralogues is capable of complementing the growth of ACBP-deficient yeast cells, and that they exhibit distinct temporal and tissue expression patterns in C. elegans. We have obtained loss-of-function mutants for six of these forms. All single mutants display relatively subtle phenotypes; however, we find that functional loss of ACBP-1 leads to reduced triacylglycerol (triglyceride) levels and aberrant lipid droplet morphology and number in the intestine. We also show that worms lacking ACBP-2 show a severe decrease in the β-oxidation of unsaturated fatty acids. A quadruple mutant, lacking all basal ACBPs, is slightly developmentally delayed, displays abnormal intestinal lipid storage, and increased β-oxidation. Collectively, the present results suggest that each of the ACBP paralogues serves a distinct function in C. elegans.

scholarly journals Estrogen receptor-related receptors in the killifish Fundulus heteroclitus: diversity, expression, and estrogen responsiveness

2006 ◽  
Vol 37 (1) ◽  
pp. 105-120 ◽  
Author(s):  
A M Tarrant ◽  
S R Greytak ◽  
G V Callard ◽  
M E Hahn
Keyword(s):  
Estrogen Receptor ◽  
Fundulus Heteroclitus ◽  
Sequence Similarity ◽  
Mammalian Species ◽  
Expression Patterns ◽  
Tissue Expression ◽  
Placental Development ◽  
Physiological Processes ◽  
Estrogen Exposure ◽  
Mammalian Tissues

The estrogen receptor-related receptors (ERRs) are a group of nuclear receptors that were originally identified on the basis of sequence similarity to the estrogen receptors. The three mammalian ERR genes have been implicated in diverse physiological processes ranging from placental development to maintenance of bone density, but the diversity, function, and regulation of ERRs in non-mammalian species are not well understood. In this study, we report the cloning of four ERR cDNAs from the Atlantic killifish, Fundulus heteroclitus, along with adult tissue expression and estrogen responsiveness. Phylogenetic analysis indicates that F. heteroclitus (Fh)ERRα is an ortholog of the single ERRα identified in mammals, pufferfish, and zebrafish. FhERRβa and FhERRβb are co-orthologs of the mammalian ERRβ. Phylogenetic placement of the fourth killifish ERR gene, tentatively identified as FhERRγb, is less clear. The four ERRs showed distinct, partially overlapping mRNA expression patterns in adult tissues. FhERRα was broadly expressed. FhERRβa was expressed at apparently low levels in eye, brain, and ovary. FhERRβb was expressed more broadly in liver, gonad, eye, brain, and kidney. FhERRγb was expressed in multiple tissues including gill, heart, kidney, and eye. Distinct expression patterns of FhERRβa and FhERRβb are consistent with subfunctionalization of the ERRβ paralogs. Induction of ERRα mRNA by exogenous estrogen exposure has been reported in some mammalian tissues. In adult male killifish, ERR expression did not significantly change following estradiol injection, but showed a trend toward a slight induction (three- to five-fold) of ERRα expression in heart. In a second, more targeted experiment, expression of ERRα in adult female killifish was downregulated 2.5-fold in the heart following estradiol injection. In summary, our results indicate that killifish contain additional ERR genes relative to mammals, including ERRβ paralogs. In addition, regulation of ERRα expression in killifish apparently differs from regulation in mammals. Together, these features may facilitate determination of both conserved and specialized ERR gene functions.

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