scholarly journals Expression of a Gene Encoding Trypanosoma congolense Putative Abc1 Family Protein is Developmentally Regulated

2005 ◽  
Vol 67 (2) ◽  
pp. 157-164 ◽  
Author(s):  
Waren N. BATICADOS ◽  
William H. WITOLA ◽  
Noboru INOUE ◽  
Jung-Yeon, KIM ◽  
Noritaka KUBOKI ◽  
...  
Keyword(s):  
Trypanosoma Congolense ◽  
Developmentally Regulated ◽  
Gene Encoding ◽  
Family Protein

The developmentally regulated ECM glycoprotein ISG plays an essential role in organizing the ECM and orienting the cells of Volvox

2000 ◽  
Vol 113 (24) ◽  
pp. 4605-4617
Author(s):  
A. Hallmann ◽  
D.L. Kirk
Keyword(s):  
Critical Role ◽  
Somatic Cells ◽  
Cell Types ◽  
Model System ◽  
Swimming Behavior ◽  
Truncated Form ◽  
Developmentally Regulated ◽  
Gene Encoding ◽  
Ecm Architecture ◽  
Multicellular Organisms

Volvox is one of the simplest multicellular organisms with only two cell types, yet it has a surprisingly complex extracellular matrix (ECM) containing many region-specific morphological components, making Volvox suitable as a model system for ECM investigations. ECM deposition begins shortly after inversion, which is the process by which the embryo turns itself right-side-out at the end of embryogenesis. It was previously shown that the gene encoding an ECM glycoprotein called ISG is transcribed very transiently during inversion. Here we show that the developmentally controlled ISG accumulates at the bases of the flagella right after inversion, before any morphologically recognizable ECM structures have yet developed. Later, ISG is abundant in the ‘flagellar hillocks’ that encircle the basal ends of all flagella, and in the adjacent ‘boundary zone’ that delimits the spheroid. Transgenic Volvox were generated which express a truncated form of ISG. These transgenics exhibit a severely disorganized ECM within which the cells are embedded in a highly chaotic manner that precludes motility. A synthetic version of the C-terminal decapeptide of ISG has a similar disorganizing effect, but only when it is applied during or shortly after inversion. We postulate that ISG plays a critical role in morphogenesis and acts as a key organizer of ECM architecture; at the very beginning of ECM formation ISG establishes an essential initial framework that both holds the somatic cells in an adaptive orientation and acts as the scaffold upon which the rest of the ECM can be properly assembled, assuring that somatic cells of post-inversion spheroids are held in orientations and locations that makes adaptive swimming behavior possible.

scholarly journals BrucellaPeriplasmic Protein EipB Is a Molecular Determinant of Cell Envelope Integrity and Virulence

2019 ◽  
Vol 201 (12) ◽  
Author(s):  
Julien Herrou ◽  
Jonathan W. Willett ◽  
Aretha Fiebig ◽  
Daniel M. Czyż ◽  
Jason X. Cheng ◽  
...  
Keyword(s):  
Cell Envelope ◽  
Mammalian Host ◽  
Periplasmic Protein ◽  
Periplasmic Space ◽  
Gene Encoding ◽  
Tetratricopeptide Repeats ◽  
Content Type ◽  
Family Protein ◽  
Synthetically Lethal

ABSTRACTThe Gram-negative cell envelope is a remarkable structure with core components that include an inner membrane, an outer membrane, and a peptidoglycan layer in the periplasmic space between. Multiple molecular systems function to maintain integrity of this essential barrier between the interior of the cell and its surrounding environment. We show that a conserved DUF1849 family protein, EipB, is secreted to the periplasmic space ofBrucellaspecies, a monophyletic group of intracellular pathogens. In the periplasm, EipB folds into an unusual 14-stranded β-spiral structure that resembles the LolA and LolB lipoprotein delivery system, though the overall fold of EipB is distinct from LolA/LolB. Deletion ofeipBresults in defects inBrucellacell envelope integrityin vitroand in maintenance of spleen colonization in a mouse model ofBrucella abortusinfection. Transposon disruption ofttpA, which encodes a periplasmic protein containing tetratricopeptide repeats, is synthetically lethal witheipBdeletion.ttpAis a reported virulence determinant inBrucella, and our studies ofttpAdeletion and overexpression strains provide evidence that this gene also contributes to cell envelope function. We conclude thateipBandttpAfunction in theBrucellaperiplasmic space to maintain cell envelope integrity, which facilitates survival in a mammalian host.IMPORTANCEBrucellaspecies cause brucellosis, a global zoonosis. A gene encoding a conserved DUF1849-family protein, which we have named EipB, is present in all sequencedBrucellaand several other genera in the classAlphaproteobacteria. The manuscript provides the first functional and structural characterization of a DUF1849 protein. We show that EipB is secreted to the periplasm where it forms a spiral-shaped antiparallel β protein that is a determinant of cell envelope integrityin vitroand virulence in an animal model of disease.eipBgenetically interacts withttpA, which also encodes a periplasmic protein. We propose that EipB and TtpA function as part of a system required for cell envelope homeostasis in selectAlphaproteobacteria.

scholarly journals Salivary (SD-Type) Cystatins: Over One Billion Years in the Making—But to What Purpose?

2002 ◽  
Vol 13 (6) ◽  
pp. 485-508 ◽  
Author(s):  
D.P. Dickinson
Keyword(s):  
Structure Function ◽  
Submandibular Gland ◽  
Cystatin C ◽  
Housekeeping Gene ◽  
Human Saliva ◽  
Protein Family ◽  
The Body ◽  
Developmentally Regulated ◽  
Gene Encoding ◽  
Cysteine Peptidases

Human saliva contains relatively abundant proteins that are related ancestrally in sequence to the cystatin superfamily. Most, although not all, members of this superfamily are potent inhibitors of cysteine peptidases. Four related genes have been identified, CST1, 2, 4 and 5, encoding cystatins SN, SA, S, and D, respectively. CST1, 4, and probably CST5 are now known to be expressed in a limited number of other tissues in the body, primarily in exocrine epithelia, and the term SD-type cystatin is more appropriate than ’salivary cystatin’. These genes are co-ordinately regulated in the submandibular gland during post-natal development. The organization of these tissue-specifically-expressed genes in the genome, and their phylogeny, indicate that they evolved from an ancestral housekeeping gene encoding the ubiquitously expressed cystatin C, and are members of a larger protein family. Their relationship to rat cystatin S, a developmentally regulated rodent submandibular gland protein, remains to be established. In this review, the evolution of the SD-type cystatins in the cystatin superfamily, their genomics, expression, and structure-function relationships are examined and compared with known cystatin functions, with the goal of providing clues to their biological roles.

Pear IAA1 gene encoding an auxin-responsive Aux/IAA protein is involved in fruit development and response to salicylic acid

2014 ◽  
Vol 94 (2) ◽  
pp. 263-271 ◽  
Author(s):  
Haiyan Shi ◽  
Yanhui Wang ◽  
Zhenghong Li ◽  
Diansheng Zhang ◽  
Yufeng Zhang ◽  
...  
Keyword(s):  
Salicylic Acid ◽  
Fruit Development ◽  
Phylogenetic Analyses ◽  
Pcr Amplification ◽  
Pyrus Pyrifolia ◽  
Dimerization Domain ◽  
Developmentally Regulated ◽  
Gene Encoding ◽  
Domain Profile ◽  
Localization Signal

Shi, H., Wang, Y., Li, Z., Zhang, D., Zhang, Y., Xiang, D., Li, Y. and Zhang, Y. 2014. Pear IAA1 gene encoding an auxin-responsive Aux/IAA protein is involved in fruit development and response to salicylic acid. Can. J. Plant Sci. 94: 263–271. Auxin-responsive Aux/IAA proteins are rapidly auxin-induced, short-lived proteins that act as repressors for the auxin response factor (ARF)-activated gene expression. A gene encoding an Aux/IAA protein and designated PpIAA1 was isolated from pear (Pyrus pyrifolia). Using PCR amplification techniques, the genomic clone corresponding to PpIAA1 was isolated and shown to contain three introns with typical GT/AG boundaries defining the splice junctions. The deduced PpIAA1 protein contains the conserved features of indole-3-acetic acids (IAA): four Aux/IAA conserved domains, Aux/IAA family domain, Aux/IAA-ARF dimerization domain profile, and conserved nuclear localization signal (NLS) motifs. Phylogenetic analyses clearly demonstrated PpIAA1 has the highest homology with grape VvIAA. PpIAA1 was preferentially expressed in fruit, and moderate expression was found in anthers. Relatively low expression signal was detected in other tissues including shoots, leaves, and petals. Moreover, expression of PpIAA1 was developmentally regulated in fruit. Further study demonstrated that PpIAA1 expression in pear fruit was remarkably regulated by salicylic acid and IAA. The data suggest that PpIAA1 might be involved in the interplay between IAA and salicylic acid signaling pathway during the fruit development of pear.

scholarly journals A Gene Encoding Proline Dehydrogenase Is Not Only Induced by Proline and Hypoosmolarity, but Is Also Developmentally Regulated in the Reproductive Organs of Arabidopsis

1998 ◽  
Vol 118 (4) ◽  
pp. 1233-1241 ◽  
Author(s):  
Kazuo Nakashima ◽  
Rie Satoh ◽  
Tomohiro Kiyosue ◽  
Kazuko Yamaguchi-Shinozaki ◽  
Kazuo Shinozaki
Keyword(s):  
Reproductive Organs ◽  
Proline Dehydrogenase ◽  
Developmentally Regulated ◽  
Gene Encoding

Evidence for the presence of an NF-kappaB signal transduction system in Dictyostelium discoideum

1999 ◽  
Vol 112 (20) ◽  
pp. 3529-3535 ◽  
Author(s):  
F. Traincard ◽  
E. Ponte ◽  
J. Pun ◽  
B. Coukell ◽  
M. Veron
Keyword(s):  
Signal Transduction ◽  
Transcription Factors ◽  
Dictyostelium Discoideum ◽  
Nuclear Translocation ◽  
Developmental Process ◽  
Signal Transduction System ◽  
Developmentally Regulated ◽  
Gene Encoding ◽  
Nuclear Extracts ◽  
Nf Kappab

The Rel/NF-kappaB family of transcription factors and regulators has so far only been described in vertebrates and arthropods, where they mediate responses to many extracellular signals. No counterparts of genes coding for such proteins have been identified in the Caenorhabditis elegans genome and no NF-kappaB activity was found in Saccharomyces cerevisiae. We describe here the presence of an NF-kappaB transduction pathway in the lower eukaryote Dictyostelium discoideum. Using antibodies raised against components of the mammalian NF-kappaB pathway, we demonstrate in Dictyostelium cells extracts the presence of proteins homologous to Rel/NF-kappaB, IkappaB and IKK components. Using gel-shift experiments in nuclear extracts of developing Dictyostelium cells, we demonstrate the presence of proteins binding to kappaB consensus oligonucleotides and to a GC-rich kappaB-like sequence, lying in the promoter of cbpA, a developmentally regulated Dictyostelium gene encoding the Ca(2+)-binding protein CBP1. Using immunofluorescence, we show specific nuclear translocation of the p65 and p50 homologues of the NF-kappaB transcription factors as vegetatively growing cells develop to the slug stage. Taken together, our results strongly indicate the presence of a complete NF-kappaB signal transduction system in Dictyostelium discoideum that could be involved in the developmental process.

scholarly journals Molecular genetic characterization of a developmentally regulated human perinatal myosin heavy chain.

1989 ◽  
Vol 108 (5) ◽  
pp. 1791-1797 ◽  
Author(s):  
R Feghali ◽  
L A Leinwand
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Molecular Genetic ◽  
Amino Acid Sequences ◽  
Developmentally Regulated ◽  
Gene Encoding ◽  
Cdna Insert ◽  
Myosin Heavy Chain Isoform ◽  
Skeletal Tissue ◽  
Ribonuclease Protection

We have isolated a human cDNA which corresponds to a developmentally regulated sarcomeric myosin heavy chain. RNA hybridization and DNA sequence analysis indicate that this cDNA, called SMHCP, encodes a perinatal myosin heavy chain isoform. The nucleotide and deduced amino acid sequences of the 3.4-kb cDNA insert show strong homology with other sarcomeric myosin heavy chains. The strongest homology is to a previously described 970-bp cDNA encoding a rat perinatal isoform (Periasamy, M., D. F. Wieczorek, and B. Nadal-Ginard. 1984. J. Biol. Chem. 259:13573-13578). The homology between the analogous human and rat perinatal myosin heavy chain cDNAs is maintained through the highly isoform-specific final 20 carboxyl-terminal amino acids, as well as the 3' untranslated region. Ribonuclease protection studies show that the mRNA encoding this isoform is expressed at high levels in 21-wk fetal skeletal tissue and not in fetal cardiac muscle. In contrast to the rat perinatal isoform, which was not found to be expressed in adult hind-leg tissue, the gene encoding SMHCP continues to be expressed in adult human skeletal tissue, but at lower levels relative to fetal skeletal tissue.

scholarly journals The SUMO Pathway Is Developmentally Regulated and Required for Programmed DNA Elimination in Paramecium tetraurelia

2006 ◽  
Vol 5 (5) ◽  
pp. 806-815 ◽  
Author(s):  
Atsushi Matsuda ◽  
James D. Forney
Keyword(s):  
Sexual Reproduction ◽  
Germ Line ◽  
Developmental Regulation ◽  
Dna Amplification ◽  
Northern Analysis ◽  
Paramecium Tetraurelia ◽  
Developmentally Regulated ◽  
Gene Encoding ◽  
Dna Elimination ◽  
Sumo Pathway

ABSTRACT Extensive genome-wide remodeling occurs during the formation of the somatic macronuclei from the germ line micronuclei in ciliated protozoa. This process is limited to sexual reproduction and includes DNA amplification, chromosome fragmentation, and the elimination of internal segments of DNA. Our efforts to define the pathways regulating these events revealed a gene encoding a homologue of ubiquitin activating enzyme 2 (UBA2) that is upregulated at the onset of macronuclear development in Paramecium tetraurelia. Uba2 enzymes are known to activate the protein called small ubiquitin-related modifier (SUMO) that is covalently attached to target proteins. Consistent with this relationship, Northern analysis showed increased abundance of SUMO transcripts during sexual reproduction in Paramecium. RNA interference (RNAi) against UBA2 or SUMO during vegetative growth had little effect on cell survival or fission rates. In contrast, RNAi of mating cells resulted in failure to form a functional macronucleus. Despite normal amplification of the genome, excision of internal eliminated sequences was completely blocked. Additional experiments showed that the homologous UBA2 and SUMO genes in Tetrahymena thermophila are also upregulated during conjugation. These results provide evidence for the developmental regulation of the SUMO pathway in ciliates and suggest a key role for the pathway in controlling genome remodeling.

scholarly journals Structure and expression of murine mgcRacGAP: its developmental regulation suggests a role for the Rac/MgcRacGAP signalling pathway in neurogenesis

1999 ◽  
Vol 343 (1) ◽  
pp. 225-230 ◽  
Author(s):  
Chantal ARAR ◽  
Marie-Odile OTT ◽  
Aminata TOURÉ ◽  
Gérard GACON
Keyword(s):  
Germ Cells ◽  
Developmental Regulation ◽  
Ventricular Zone ◽  
Developmentally Regulated ◽  
Gene Encoding ◽  
Male Germ Cells ◽  
Preferential Expression ◽  
Wide Range ◽  
Developing Neurons

Rho-family GTPases regulate a wide range of biological functions including cell migration, cell adhesion and cell growth. Recently, results from studies in vivo in Drosophila, mouse and humans have demonstrated the involvement of these GTPases in mechanisms controlling neuronal differentiation and the development of the central nervous system (CNS). However, the signalling pathways underlying these functions and the proteins directly regulating RhoGTPases in developing neurons are poorly defined. Here we report the structure and expression pattern of the murine orthologue of mgcRacGAP, a human gene encoding a RacGTPase partner expressed in male germ cells [Touré, Dorseuil, Morin, Timmons, Jegou, Reibel and Gacon (1998) J. Biol. Chem. 273, 6019-6023]. In contrast with that from humans, murine mgcRacGAP encodes two distinct transcripts. Both are developmentally regulated. A 2.2 kb transcript is strongly expressed in mature testis and is up-regulated with spermatogenesis. A 3 kb RNA is predominant in the embryo and is expressed primarily in the CNS during the neurogenic phase, decreasing after birth. In situ hybridization analysis in embryonic-day 14.5 mouse embryos demonstrates a preferential expression of mgcRacGAP in the proliferative ventricular zone of the cortex. In addition to the expression of mgcRacGAP in male germ cells already reported in humans and suggesting an involvement in spermatogenesis, we characterize an embryonic transcript whose expression is closely correlated with neurogenesis. This result addresses the question of the role of Rac/MgcRacGAP pathway in neuronal proliferation.

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