scholarly journals Identification and Characterization of a Determinant (eep) on the Enterococcus faecalisChromosome That Is Involved in Production of the Peptide Sex Pheromone cAD1

1999 ◽  
Vol 181 (19) ◽  
pp. 5915-5921 ◽  
Author(s):  
Florence Y. An ◽  
Mark C. Sulavik ◽  
Don B. Clewell
Keyword(s):  
Sex Pheromone ◽  
Wild Type ◽  
Mating Response ◽  
Enhanced Production ◽  
Precursor Structure ◽  
Enhanced Expression ◽  
Membrane Spanning ◽  
Identification And Characterization ◽  
Free Strains

ABSTRACT Plasmid-free strains of Enterococcus faecalis secrete a peptide sex pheromone, cAD1, which specifically induces a mating response by donors carrying the hemolysin plasmid pAD1 or related elements. A determinant on the E. faecalis OG1X chromosome has been found to encode a 46.5-kDa protein that plays an important role in the production of the extracellular cAD1. Wild-type E. faecalis OG1X cells harboring a plasmid chimera carrying the determinant exhibited an eightfold enhanced production of cAD1, and plasmid-free cells carrying a mutated chromosomal determinant secreted undetectable or very low amounts of the pheromone. The production of other pheromones such as cPD1, cOB1, and cCF10 was also influenced, although there was no effect on the pheromone cAM373. The determinant, designated eep (for enhanced expression of pheromone), did not include the sequence of the pheromone. Its deduced product (Eep) contains apparent membrane-spanning sequences; conceivably it is involved in processing a pheromone precursor structure or in some way regulates expression or secretion.

scholarly journals Genome-Wide Identification and Characterization of CIPK Family and Analysis Responses to Various Stresses in Apple (Malus domestica)

2018 ◽  
Vol 19 (7) ◽  
pp. 2131 ◽  
Author(s):  
Lili Niu ◽  
Biying Dong ◽  
Zhihua Song ◽  
Dong Meng ◽  
Yujie Fu
Keyword(s):  
Growth Stages ◽  
Hormone Signaling ◽  
Chromosomal Distribution ◽  
Interacting Protein ◽  
C Terminus ◽  
Genome Wide ◽  
Enhanced Expression ◽  
Interaction Domains ◽  
Identification And Characterization

In the CIPK family, the CBL-interacting protein kinases have shown crucial roles in hormone signaling transduction, and response to abiotic stress in plant developmental processes. The CIPK family is characterized by conserved NAF/FISL (Asn-Ala-Phe) and PPI (protein-phosphatase interaction) domains in the C-terminus. However, little data has been reported about the CIPK family in apple. A total of 34 MdCIPK genes were identified from the apple genome in this study and were later divided into two groups according to the CIPK domains, characterized by gene structure and chromosomal distribution, and then mapped onto 17 chromosomes. All MdCIPK genes were expressed in the four apple tissues (leaf, root, flower, and fruit). In addition, the MdCIPK gene expression profile showed that five members among them revealed enhanced expression during the pollen tube growth stages. The MdCIPK4 was the most expressive during the entire fruit development stages. Under stress conditions 21 MdCIPK genes transcript levels were up-regulated in response to fungal and salt treatments. This suggested the possible features of these genes’ response to stresses in apples. Our findings provide a new insight about the roles of CIPK genes in apples, which could contribute to the cloning and functional analysis of CIPK genes in the future.

scholarly journals Identification and Characterization of the Phage Gene sav, Involved in Sensitivity to the Lactococcal Abortive Infection Mechanism AbiV

2009 ◽  
Vol 75 (8) ◽  
pp. 2484-2494 ◽  
Author(s):  
Jakob Haaber ◽  
Geneviève M. Rousseau ◽  
Karin Hammer ◽  
Sylvain Moineau
Keyword(s):  
Gel Filtration ◽  
Point Mutations ◽  
Whole Genome ◽  
Wild Type ◽  
Abortive Infection ◽  
Native Form ◽  
Phage Gene ◽  
Infection Mechanism ◽  
Identification And Characterization

ABSTRACT Lactococcus lactis phage mutants that are insensitive to the recently characterized abortive infection mechanism AbiV were isolated and analyzed in an effort to elucidate factors involved in the sensitivity to AbiV. Whole-genome sequencing of the phage mutants p2.1 and p2.2 revealed mutations in an orf that is transcribed early, indicating that this orf was responsible for AbiV sensitivity. Sequencing of the homologous regions in the genomes of other AbiV-insensitive mutants derived from p2 and six other lactococcal wild-type phages revealed point mutations in the homologous orf sequences. The orf was named sav (for sensitivity to AbiV), and the encoded polypeptide was named SaV. The purification of a His-tagged SaV polypeptide by gel filtration suggested that the polypeptide formed a dimer in its native form. The overexpression of SaV in L. lactis and Escherichia coli led to a rapid toxic effect. Conserved, evolutionarily related regions in SaV polypeptides of different phage groups are likely to be responsible for the AbiV-sensitive phenotype and the toxicity.

scholarly journals Identification and Characterization of a New Lipoprotein, NlpI, in Escherichia coli K-12

1999 ◽  
Vol 181 (14) ◽  
pp. 4318-4325 ◽  
Author(s):  
Masaru Ohara ◽  
Henry C. Wu ◽  
Krishnan Sankaran ◽  
Paul D. Rick
Keyword(s):  
Escherichia Coli ◽  
Direct Consequence ◽  
Insertion Mutant ◽  
Polynucleotide Phosphorylase ◽  
Wild Type ◽  
E Coli ◽  
K 12 ◽  
Identification And Characterization ◽  
Lines Of Evidence

ABSTRACT We report here the identification of a new lipoprotein, NlpI, inEscherichia coli K-12. The NlpI structural gene (nlpI) is located between the genes pnp(polynucleotide phosphorylase) and deaD (RNA helicase) at 71 min on the E. coli chromosome. The nlpI gene encodes a putative polypeptide of approximately 34 kDa, and multiple lines of evidence clearly demonstrate that NlpI is indeed a lipoprotein. An nlpI::cm mutation rendered growth of the cells osmotically sensitive, and incubation of the insertion mutant at an elevated temperature resulted in the formation of filaments. The altered phenotype of the mutant was a direct consequence of the mutation in nlpI, since it was complemented by the wild-type nlpI gene alone. Overexpression of the unaltered nlpI gene in wild-type cells resulted in the loss of the rod morphology and the formation of single prolate ellipsoids and pairs of prolate ellipsoids joined by partial constrictions. NlpI may be important for an as-yet-undefined step in the overall process of cell division.

scholarly journals Identification and Characterization of a Phase-Variable Nonfimbrial Salmonella typhimurium Gene That Alters O-Antigen Production

1998 ◽  
Vol 66 (12) ◽  
pp. 5725-5730 ◽  
Author(s):  
Lola Y. Kwan ◽  
Richard E. Isaacson
Keyword(s):  
Salmonella Typhimurium ◽  
Phenotypic Switching ◽  
Phase Variable ◽  
Wild Type ◽  
Phagocytic Cells ◽  
Antigen Production ◽  
O Antigen ◽  
Identification And Characterization ◽  
Wild Type Parent

ABSTRACT Salmonella typhimurium 798, which was isolated from a pig, is known to phase vary from a nonadhesive to an adhesive phenotype. Cells of the adhesive phenotype adhere to porcine enterocytes, are more readily phagocytized by porcine neutrophils and macrophages, and once phagocytized can survive intracellularly, while cells of the nonadhesive phenotype die rapidly. The effect of phenotypic switching also can be visualized by changes in colony morphologies and the presence of between 10 and 15 proteins in the envelopes of cells in the adhesive phenotype. Mutants previously constructed with cells in the adhesive phenotype and the transposon TnphoA were screened to identify mutants lacking one or more of the unique proteins. One mutation was cloned and sequenced, and the mutation was shown to be in rfaL (O-antigen ligase). Expression of O antigen was shown to be phase variable. The adhesive strain expressed an O antigen that was at least eightfold longer than that for the nonadhesive strain and by virtue of O-antigen production was resistant to porcine complement. The mutant survived intracellularly in phagocytic cells as well as its wild-type parent.

scholarly journals Identification and Characterization of a Novel Competence Gene,comC, Required for DNA Binding and Uptake inAcinetobacter sp. Strain BD413

1998 ◽  
Vol 180 (6) ◽  
pp. 1592-1595 ◽  
Author(s):  
Caroline Link ◽  
Sandra Eickernjäger ◽  
Dirk Porstendörfer ◽  
Beate Averhoff
Keyword(s):  
Electron Microscopy ◽  
Dna Binding ◽  
Natural Transformation ◽  
Leader Sequence ◽  
Wild Type ◽  
Type Iv Pilus ◽  
Competence Gene ◽  
Type Iv ◽  
Identification And Characterization

ABSTRACT A gene (comC) essential for natural transformation was identified in Acinetobacter sp. strain BD413. ComC has a typical leader sequence and is similar to different type IV pilus assembly factors. A comC mutant (T308) is not able to bind or take up DNA but exhibits a piliation phenotype indistinguishable from the transformation wild type as revealed by electron microscopy.

scholarly journals Identification and Characterization of the Bacillus thuringiensis phaZ Gene, Encoding New Intracellular Poly-3-Hydroxybutyrate Depolymerase

2006 ◽  
Vol 188 (21) ◽  
pp. 7592-7599 ◽  
Author(s):  
Chi-Ling Tseng ◽  
Hui-Ju Chen ◽  
Gwo-Chyuan Shaw
Keyword(s):  
Bacillus Thuringiensis ◽  
Wild Type ◽  
Gene Encoding ◽  
Significant Similarity ◽  
Phb Depolymerase ◽  
New Type ◽  
Identification And Characterization

ABSTRACTA gene that codes for a novel intracellular poly-3-hydroxybutyrate (PHB) depolymerase has now been identified in the genome ofBacillus thuringiensissubsp.israelensisATCC 35646. This gene, previously annotated as a hypothetical 3-oxoadipate enol-lactonase (PcaD) gene and now designatedphaZ, encodes a protein that shows no significant similarity with any known PHB depolymerase. Purified His-tagged PhaZ could efficiently degrade trypsin-activated native PHB granules as well as artificial amorphous PHB granules and release 3-hydroxybutyrate monomer as a hydrolytic product, but it could not hydrolyze denatured semicrystalline PHB. In contrast, purified His-tagged PcaD ofPseudomonas putidawas unable to degrade trypsin-activated native PHB granules and artificial amorphous PHB granules. TheB. thuringiensisPhaZ was inactive againstp-nitrophenylpalmitate, tributyrin, and triolein. Sonication supernatants of the wild-typeB. thuringiensiscells exhibited a PHB-hydrolyzing activity in vitro, whereas those prepared from aphaZmutant lost this activity. ThephaZmutant showed a higher PHB content than the wild type at late stationary phase of growth in a nutrient-rich medium, indicating that this PhaZ can function as a PHB depolymerase in vivo. PhaZ contains a lipase box-like sequence (G-W-S102-M-G) but lacks a signal peptide. A purified His-tagged S102A variant had lost the PHB-hydrolyzing activity. Taken together, these results indicate thatB. thuringiensisharbors a new type of intracellular PHB depolymerase.

scholarly journals takeout, a Novel DrosophilaGene under Circadian Clock Transcriptional Regulation

2000 ◽  
Vol 20 (18) ◽  
pp. 6935-6944 ◽  
Author(s):  
W. Venus So ◽  
Lea Sarov-Blat ◽  
Carolyn K. Kotarski ◽  
Michael J. McDonald ◽  
Ravi Allada ◽  
...  
Keyword(s):  
Gene Expression ◽  
Transcriptional Regulation ◽  
Transcription Factors ◽  
Gene Family ◽  
Wild Type ◽  
Circadian Control ◽  
Its Gene ◽  
E Box ◽  
Identification And Characterization

ABSTRACT We report the identification and characterization of a newDrosophila clock-regulated gene, takeout(to). to is a member of a novel gene family and is implicated in circadian control of feeding behavior. Its gene expression is down-regulated in all of the clock mutants tested. In wild-type flies, to mRNA exhibits daily cycling expression but with a novel phase, delayed relative to those of the better-characterized clock mRNAs, period andtimeless. The E-box-containing sequence in theto promoter shows impressive similarities with those ofperiod and timeless. However, our results suggest that the E box is not involved in the amplitude and phase of the transcriptional cycling of to. The circadian delayed transcriptional phase is therefore most likely the result of indirect regulation through unknown transcription factors.

scholarly journals A Mutation in CsHY2 Encoding a Phytochromobilin (PΦB) Synthase Leads to an Elongated Hypocotyl 1(elh1) Phenotype in Cucumber (Cucumis sativus L.)

2021 ◽  
Author(s):  
Liangliang Hu ◽  
Peng Liu ◽  
Zhuoshuai Jin ◽  
Jing Sun ◽  
Yiqun Weng ◽  
...  
Keyword(s):  
Cell Elongation ◽  
Ectopic Expression ◽  
Rna Seq ◽  
Wild Type ◽  
Hypocotyl Growth ◽  
Hypocotyl Length ◽  
Critical Determinant ◽  
Cucumis Sativus L ◽  
Identification And Characterization

Abstract Hypocotyl length is a critical determinant in establishing high quality seedlings for successful cucumber production, but knowledge on the molecular regulation of hypocotyl growth in cucumber is very limited. Here we reported identification and characterization of a cucumber elongated hypocotyl 1 (elh1) mutant. We found that the longer hypocotyl in elh1 was due to longitudinal growth of hypocotyl cells. With fine mapping, the elh1 locus was delimited to a 20.9-kb region containing three annotated genes; only one polymorphism was identified in this region between two parental lines, which was a non-synonymous SNP (G28153633A) in the third exon of CsHY2 (CsGy1G030000) that encodes a phytochromobilin (PΦB) synthase. Uniqueness of the mutant allele at CsHY2 was verified in 515 cucumber lines. Ectopic expression of CsHY2 in Arabidopsis hy2-1 mutant led to reduced hypocotyl length. The PΦB protein was targeted to chloroplasts. The expression levels of CsHY2 and five phytochrome genes, CsPHYA1, CsPHYA2, CsPHYB, CsPHYC and CsPHYE were all significantly down-regulated while several cell elongation related genes were up-regulated in elh1 mutant compared to wild type cucumber, which are correlated with dynamic hypocotyl elongation in the mutant. RNA-seq analysis in the WT and mutant revealed differentially expressed genes involved in porphyrin and chlorophyll metabolisms, cell elongation, and plant hormone signal transduction pathways. This is the first report to characterize and clone the CsHY2 gene in cucumber. This work reveals the important of CsHY2 in regulating hypocotyl length and extends our understanding of the roles of CsHY2 in cucumber.

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