scholarly journals Nrf1D is the first candidate secretory transcription factor in the blood plasma, with its precursor existing as a unique redox-sensitive transmembrane CNC-bZIP protein in somatic tissues

2018 ◽  
Author(s):  
Jianxin Yuan ◽  
Hongxia Wang ◽  
Shaojun Li ◽  
Yuancai Xiang ◽  
Shaofan Hu ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Blood Plasma ◽  
Leucine Zipper ◽  
Transmembrane Domain ◽  
Stop Codon ◽  
Salient Feature ◽  
Bzip Protein ◽  
Protein Levels ◽  
Somatic Tissues ◽  
Alternatively Spliced

ABSTRACTAmongst multiple distinct isoforms, Nrf1D is synthesized from translation of an alternatively-spliced transcript of Nrf1 mRNA, with a naturally-occurring deletion of its stop codon-flanking 1466 nucleotides. This molecular event leads to the reading frameshift mutation, which results in a constitutive substitution of the intact Nrf1’s C-terminal 72 amino acids (aa, covering the second half of the leucine zipper motif to C-terminal Neh3L domain) by an additional extended 80-aa stretch to generate a unique variant Nrf1D. The C-terminal extra 80-aa region of Nrf1D was identified to fold into a redox-sensitive transmembrane domain that enables it to be tightly integrated within the endoplasmic reticulum (ER) membranes. Notably, the salient feature of Nrf1D confers it to be distinguishable from prototypic Nrf1, such that Nrf1D is endowed with only a less ability than wild-type Nrf1 at mediating target gene expression. Further evidence has been presented revealing that both mRNA and protein levels of Nrf1D were detected to varying extents in somatic tissues. Surprisingly, we also found the existence of Nrf1D-derived isoforms in the blood plasma, implying that it is a candidate secretory transcription factor, although its precursor acts as an integral transmembrane-bound CNC-bZIP protein that entails dynamic topologies, before being unleashed from the ER to enter the blood plasma.

scholarly journals Nrf1D Is the First Candidate Secretory Transcription Factor in the Blood Plasma, Its Precursor Existing as a Unique Redox-Sensitive Transmembrane CNC-bZIP Protein in Hemopoietic and Somatic Tissues

2018 ◽  
Vol 19 (10) ◽  
pp. 2940 ◽  
Author(s):  
Jianxin Yuan ◽  
Hongxia Wang ◽  
Yuancai Xiang ◽  
Shaofan Hu ◽  
Shaojun Li ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Blood Plasma ◽  
Leucine Zipper ◽  
Transmembrane Domain ◽  
De Novo ◽  
Stop Codon ◽  
Salient Feature ◽  
Bzip Protein ◽  
Protein Levels ◽  
Somatic Tissues

Among multiple distinct isoforms, Nrf1D is synthesized from a de novo translation of an alternatively-spliced transcript of Nrf1 mRNA, as accompanied by a naturally-occurring deletion of its stop codon-flanking 1466 nucleotides. This molecular event leads to the generation of a reading frameshift mutation, which results in a constitutive substitution of the intact Nrf1’s C-terminal 72 amino acids (aa, covering the second half of the leucine zipper motif to C-terminal Neh3L domain) by an additional extended 80-aa stretch to generate a unique variant Nrf1D. The C-terminal extra 80-aa region of Nrf1D was herein identified to be folded into a redox-sensitive transmembrane domain, enabling it to be tightly integrated within the endoplasmic reticulum (ER) membranes. Notably, the salient feature of Nrf1D enables it to be distinguishable from prototypic Nrf1, such that Nrf1D is endowed with a lesser ability than wild-type Nrf1 to mediate target gene expression. Further evidence has also been presented revealing that both mRNA and protein levels of Nrf1D, together with other isoforms similar to those of Nrf1, were detected to varying extents in hemopoietic and somatic tissues. Surprisingly, we found the existence of Nrf1D-derived isoforms in blood plasma, implying that it is a candidate secretory transcription factor, albeit its precursor acts as an integral transmembrane-bound CNC-bZIP protein that entails dynamic topologies across membranes, before being unleashed from the ER to enter the blood.

scholarly journals att, a target for regulation by tra2 in the testes of Drosophila melanogaster, encodes alternative RNAs and alternative proteins.

1996 ◽  
Vol 16 (8) ◽  
pp. 4222-4230 ◽  
Author(s):  
S J Madigan ◽  
P Edeen ◽  
J Esnayra ◽  
M McKeown
Keyword(s):  
Rna Processing ◽  
Transmembrane Domain ◽  
Somatic Tissue ◽  
Open Reading Frame ◽  
Graves Disease ◽  
Carrier Protein ◽  
Reading Frame ◽  
Protein Levels ◽  
Somatic Tissues ◽  
Promoter Usage

We have identified a gene, alternative testis transcripts (att), which is alternatively expressed, at both the RNA and protein levels, in testes and somatic tissues. The testis-specific RNA differs from somatic RNAs in both promoter usage and RNA processing and is dependent on the function of the transformer 2 gene. The differences between the somatic and testis RNAs have substantial consequences at the protein level. The somatic RNAs encode a protein with homology to the mammalian Graves' disease carrier proteins. The testis RNA lacks the initiation codons used in somatic tissue and encodes two different proteins. One of these begins in a testis-specific exon, uses a reading frame different from that for the somatic protein, and is completely novel. The other protein initiates translation in the frame of the somatic RNA at a Len CUG codon which is within the open reading frame for the somatic protein. This produces a novel truncated version of the Graves' disease carrier protein-like protein that lacks all sequences N terminal to the first transmembrane domain.

scholarly journals The gene structure and hypervariability of the complete Penaeus monodon Dscam gene

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Kantamas Apitanyasai ◽  
Shiao-Wei Huang ◽  
Tze Hann Ng ◽  
Shu-Ting He ◽  
Yu-Hsun Huang ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Gene Structure ◽  
Transmembrane Domain ◽  
Stop Codon ◽  
Penaeus Monodon ◽  
Cytoplasmic Tail ◽  
Extracellular Region ◽  
Alternatively Spliced ◽  
Alternatively Spliced Exons ◽  
Selection Of

Abstract Using two advanced sequencing approaches, Illumina and PacBio, we derive the entire Dscam gene from an M2 assembly of the complete Penaeus monodon genome. The P. monodon Dscam (PmDscam) gene is ~266 kbp, with a total of 44 exons, 5 of which are subject to alternative splicing. PmDscam has a conserved architectural structure consisting of an extracellular region with hypervariable Ig domains, a transmembrane domain, and a cytoplasmic tail. We show that, contrary to a previous report, there are in fact 26, 81 and 26 alternative exons in N-terminal Ig2, N-terminal Ig3 and the entirety of Ig7, respectively. We also identified two alternatively spliced exons in the cytoplasmic tail, with transmembrane domains in exon variants 32.1 and 32.2, and stop codons in exon variants 44.1 and 44.2. This means that alternative splicing is involved in the selection of the stop codon. There are also 7 non-constitutive cytoplasmic tail exons that can either be included or skipped. Alternative splicing and the non-constitutive exons together produce more than 21 million isoform combinations from one PmDscam locus in the P. monodon gene. A public-facing database that allows BLAST searches of all 175 exons in the PmDscam gene has been established at http://pmdscam.dbbs.ncku.edu.tw/.

scholarly journals Basic Leucine zipper (bZIP) transcription factor genes and their response to drought stress in ginseng, Panax ginseng C.A. Meyer

2020 ◽  
Author(s):  
Hongjie Li ◽  
Jing Chen ◽  
Qi Zhao ◽  
Yilai Han ◽  
Chunyu Sun ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Drought Stress ◽  
Leucine Zipper ◽  
Bzip Transcription Factor ◽  
Functional Categories ◽  
Basic Leucine Zipper ◽  
Abiotic And Biotic Stresses ◽  
Biotic Stresses ◽  
Transcription Factor Genes ◽  
Alternatively Spliced

Abstract Background: As a famous and important medicinal herb in the world, ginseng contains numerous bioactive components that are remarkable for mankind's health. The basic leucine zipper (bZIP) transcription factor genes play important roles in many biological processes and plant response to abiotic and biotic stresses. Nevertheless, these genes remain unknown in ginseng. Results: Here, we report 91 bZIP genes, designated as PgbZIP genes, identified from ginseng. These PgbZIP genes were alternatively spliced into 273 transcripts. Phylogenetic analysis grouped the PgbZIP genes into ten groups, including A, B, C, D, E, F, G, H, I and S. Gene Ontology (GO) categorized the PgbZIP genes into a number of functional categories, suggesting that they have substantially diversified in functionality, even though their putative proteins share a number of conserved motifs. These 273 PgbZIP transcripts expressed quite differentially across 14 different tissues, the roots of different aged, and the roots of different cultivars. However, the expression of these transcripts was coordinated as they formed a co-expression network. Furthermore, we studied their response to drought stress in ginseng using five representatives of the PgbZIP genes, including PgbZIP25 , PgbZIP38 , PgbZIP39 , PgbZIP53 and PgbZIP54 . The results showed that these PgbZIP genes all responded to drought stress in ginseng, but the magnitudes of their response to drought stress varied. Conclusions: These results provide knowledge and resources for deeper functional analysis of PgbZIP genes and molecular tools for enhanced drought tolerance breeding in ginseng.

scholarly journals Mammalian Transcription Factor ATF6 Is Synthesized as a Transmembrane Protein and Activated by Proteolysis in Response to Endoplasmic Reticulum Stress

1999 ◽  
Vol 10 (11) ◽  
pp. 3787-3799 ◽  
Author(s):  
Kyosuke Haze ◽  
Hiderou Yoshida ◽  
Hideki Yanagi ◽  
Takashi Yura ◽  
Kazutoshi Mori
Keyword(s):  
Endoplasmic Reticulum ◽  
Transcription Factor ◽  
Leucine Zipper ◽  
Transmembrane Domain ◽  
Transmembrane Protein ◽  
Cholesterol Homeostasis ◽  
Basic Leucine Zipper ◽  
Transmembrane Glycoprotein ◽  
Stressed Cells ◽  
The Unfolded Protein Response

The unfolded protein response (UPR) controls the levels of molecular chaperones and enzymes involved in protein folding in the endoplasmic reticulum (ER). We recently isolated ATF6 as a candidate for mammalian UPR-specific transcription factor. We report here that ATF6 constitutively expressed as a 90-kDa protein (p90ATF6) is directly converted to a 50-kDa protein (p50ATF6) in ER-stressed cells. Furthermore, we showed that the most important consequence of this conversion was altered subcellular localization; p90ATF6 is embedded in the ER, whereas p50ATF6 is a nuclear protein. p90ATF6 is a type II transmembrane glycoprotein with a hydrophobic stretch in the middle of the molecule. Thus, the N-terminal half containing a basic leucine zipper motif is oriented facing the cytoplasm. Full-length ATF6 as well as its C-terminal deletion mutant carrying the transmembrane domain is localized in the ER when transfected. In contrast, mutant ATF6 representing the cytoplasmic region translocates into the nucleus and activates transcription of the endogenous GRP78/BiP gene. We propose that ER stress-induced proteolysis of membrane-bound p90ATF6 releases soluble p50ATF6, leading to induced transcription in the nucleus. Unlike yeast UPR, mammalian UPR appears to use a system similar to that reported for cholesterol homeostasis.

scholarly journals Basic leucine zipper (bZIP) transcription factor genes and their responses to drought stress in ginseng, Panax ginseng C.A. Meyer

BMC Genomics ◽  
2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Hongjie Li ◽  
Jing Chen ◽  
Qi Zhao ◽  
Yilai Han ◽  
Li Li ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Drought Stress ◽  
Leucine Zipper ◽  
Bzip Transcription Factor ◽  
Plant Responses ◽  
Basic Leucine Zipper ◽  
Abiotic And Biotic Stresses ◽  
Biotic Stresses ◽  
Transcription Factor Genes ◽  
Alternatively Spliced

Abstract Background Ginseng is an important medicinal herb in Asia and Northern America. The basic leucine zipper (bZIP) transcription factor genes play important roles in many biological processes and plant responses to abiotic and biotic stresses, such as drought stress. Nevertheless, the genes remain unknown in ginseng. Results Here, we report 91 bZIP genes identified from ginseng, designated PgbZIP genes. These PgbZIP genes were alternatively spliced into 273 transcripts. Phylogenetic analysis grouped the PgbZIP genes into ten groups, including A, B, C, D, E, F, G, H, I and S. Gene Ontology (GO) categorized the PgbZIP genes into five functional subcategories, suggesting that they have diversified in functionality, even though their putative proteins share a number of conserved motifs. These 273 PgbZIP transcripts expressed differentially across 14 tissues, the roots of different ages and the roots of different genotypes. However, the transcripts of the genes expressed coordinately and were more likely to form a co-expression network. Furthermore, we studied the responses of the PgbZIP genes to drought stress in ginseng using a random selection of five PgbZIP genes, including PgbZIP25, PgbZIP38, PgbZIP39, PgbZIP53 and PgbZIP54. The results showed that all five PgbZIP genes responded to drought stress in ginseng, indicating that the PgbZIP genes play important roles in ginseng responses to drought stress. Conclusions These results provide knowledge and gene resources for deeper functional analysis of the PgbZIP genes and molecular tools for enhanced drought tolerance breeding in ginseng.

Alternative Splicing Is Responsible for the Presence of Two Tissue Factor mRNA Species in LPS Stimulated Human Monocytes

1992 ◽  
Vol 67 (02) ◽  
pp. 272-276 ◽  
Author(s):  
C Paul ◽  
E van der Logt ◽  
Pieter H Reitsma ◽  
Rogier M Bertina
Keyword(s):  
Alternative Splicing ◽  
Tissue Factor ◽  
Stop Codon ◽  
Cell Types ◽  
Northern Analysis ◽  
Human Monocytes ◽  
Mrna Species ◽  
Protein Levels ◽  
Intron 1 ◽  
Tf Gene

SummaryAlthough normally absent from the surface of all circulating cell types, tissue factor (TF) can be induced to appear on circulating monocytes by stimulants like bacterial lipopolysaccharide (LPS) and phorbolesters. Northern analysis of RNA isolated from LPS stimulated human monocytes demonstrates the presence of 2.2 kb and 3.1 kb TF mRNA species. The 2.2 kb message codes for the TF protein. As demonstrated by Northern blot analysis with a variety of TF gene probes, the 3.1 kb message arises from an alternative splicing process which fails to remove 955 bp from intron 1. Because of a stop codon in intron 1 no TF protein is produced from the 3.1 kb transcript. This larger transcript should therefore not be taken into account when comparing TF gene transcription and TF protein levels.

scholarly journals Mating Type in Chlamydomonas Is Specified by mid, the Minus-Dominance Gene

Genetics ◽  
1997 ◽  
Vol 146 (3) ◽  
pp. 859-869 ◽  
Author(s):  
Patrick J Ferris ◽  
Ursula W Goodenough
Keyword(s):  
Transcription Factor ◽  
Mating Type ◽  
Codon Bias ◽  
Leucine Zipper ◽  
Laboratory Strain ◽  
Leucine Zipper Motif ◽  
Type Locus ◽  
Diploid Cells ◽  
Necessary And Sufficient

Diploid cells of Chlamydomonas reinhardtii that are heterozygous at the mating-type locus (mt  +/mt  –) differentiate as minus gametes, a phenomenon known as minus dominance. We report the cloning and characterization of a gene that is necessary and sufficient to exert this minus dominance over the plus differentiation program. The gene, called mid, is located in the rearranged (R) domain of the mt  – locus, and has duplicated and transposed to an autosome in a laboratory strain. The imp11 mt  – mutant, which differentiates as a fusion-incompetent plus gamete, carries a point mutation in mid. Like the fus1 gene in the mt  + locus, mid displays low codon bias compared with other nuclear genes. The mid sequence carries a putative leucine zipper motif, suggesting that it functions as a transcription factor to switch on the minus program and switch off the plus program of gametic differentiation. This is the first sex-determination gene to be characterized in a green organism.

Sign in / Sign up

Export Citation Format

Share Document