scholarly journals First characterization of CLPH, a spermatid-specific protein

2009 ◽  
Vol 8 (6) ◽  
pp. 2617-2617
Author(s):  
Laura Cassiday
Keyword(s):  
Specific Protein

scholarly journals Insights into the Functionality of the Putative Residues Involved in Enterocin AS-48 Maturation

2010 ◽  
Vol 76 (21) ◽  
pp. 7268-7276 ◽  
Author(s):  
Rubén Cebrián ◽  
Mercedes Maqueda ◽  
José Luis Neira ◽  
Eva Valdivia ◽  
Manuel Martínez-Bueno ◽  
...  
Keyword(s):  
Posttranslational Modifications ◽  
High Efficiency ◽  
Specific Protein ◽  
Culture Conditions ◽  
Site Directed Mutagenesis ◽  
Circular Structure ◽  
Cleavage Enzyme ◽  
Site Recognition ◽  
Biosynthetic Machinery

ABSTRACT AS-48 is a 70-residue, α-helical, cationic bacteriocin produced by Enterococcus faecalis and is very singular in its circular structure and its broad antibacterial spectrum. The AS-48 preprotein consists of an N-terminal signal peptide (SP) (35 residues) followed by a proprotein moiety that undergoes posttranslational modifications to yield the mature and active circular protein. For the study of the specificity of the region of AS-48 that is responsible for maturation, three single mutants have been generated by site-directed mutagenesis in the as-48A structural gene. The substitutions were made just in the residues that are thought to constitute a recognition site for the SP cleavage enzyme (His-1, Met1) and in those involved in circularization (Met1, Trp70). Each derivative was expressed in the enterococcal JH2-2 strain containing the necessary native biosynthetic machinery for enterocin production. The importance of these derivatives in AS-48 processing has been evaluated on the basis of the production and structural characterization of the corresponding derivatives. Notably, only two of them (Trp70Ala and Met1Ala derivatives) could be purified in different forms and amounts and are characterized for their bactericidal activity and secondary structure. We could not detect any production of AS-48 in JH2-2(pAM401-81 His-1Ile ) by using the conventional chromatographic techniques, despite the high efficiency of the culture conditions applied to produce this enterocin. Our results underline the different important roles of the mutated residues in (i) the elimination of the SP, (ii) the production levels and antibacterial activity of the mature proteins, and (iii) protein circularization. Moreover, our findings suggest that His-1 is critically involved in cleavage site recognition, its substitution being responsible for the blockage of processing, thereby hampering the production of the specific protein in the cellular culture supernatant.

scholarly journals Characterization of an activated human ros gene.

1986 ◽  
Vol 6 (9) ◽  
pp. 3109-3116 ◽  
Author(s):  
C Birchmeier ◽  
D Birnbaum ◽  
G Waitches ◽  
O Fasano ◽  
M Wigler
Keyword(s):  
Gene Transfer ◽  
Protein Kinases ◽  
Transmembrane Domain ◽  
Extracellular Domain ◽  
Kinase Domain ◽  
Specific Protein ◽  
Normal Human

A human oncogene, mcf3, previously detected by a combination of DNA-mediated gene transfer and a tumorigenicity assay, derives from a human homology of the avian v-ros oncogene. Both v-ros and mcf3 can encode a protein with homology to tyrosine-specific protein kinases, and both mcf3 and v-ros encode a potential transmembrane domain N terminal to the kinase domain. mcf3 probably arose during gene transfer from a normal human ros gene by the loss of a putative extracellular domain. There do not appear to be any other gross rearrangements in the structure of mcf3.

scholarly journals A Novel Chromodomain Protein, Pdd3p, Associates with Internal Eliminated Sequences during Macronuclear Development inTetrahymena thermophila

2000 ◽  
Vol 20 (11) ◽  
pp. 4128-4134 ◽  
Author(s):  
Mikhail A. Nikiforov ◽  
Martin A. Gorovsky ◽  
C. David Allis
Keyword(s):  
De Novo ◽  
Germ Line ◽  
Chromosome Breakage ◽  
Specific Protein ◽  
Developmentally Regulated ◽  
Dna Elimination ◽  
Internal Eliminated Sequences ◽  
Subsequent Elimination ◽  
Rearrangement Processes

ABSTRACT Conversion of the germ line micronuclear genome into the genome of a somatic macronucleus in Tetrahymena thermophila requires several DNA rearrangement processes. These include (i) excision and subsequent elimination of several thousand internal eliminated sequences (IESs) scattered throughout the micronuclear genome and (ii) breakage of the micronuclear chromosomes into hundreds of DNA fragments, followed by de novo telomere addition to their ends. Chromosome breakage sequences (Cbs) that determine the sites of breakage and short regions of DNA adjacent to them are also eliminated. Both processes occur concomitantly in the developing macronucleus. Two stage-specific protein factors involved in germ line DNA elimination have been described previously. Pdd1p and Pdd2p (for programmed DNA degradation) physically associate with internal eliminated sequences in transient electron-dense structures in the developing macronucleus. Here, we report the purification, sequence analysis, and characterization of Pdd3p, a novel developmentally regulated, chromodomain-containing polypeptide. Pdd3p colocalizes with Pdd1p in the peripheral regions of DNA elimination structures, but is also found more internally. DNA cross-linked and immunoprecipitated with Pdd1p- or Pdd3p-specific antibodies is enriched in IESs, but not Cbs, suggesting that different protein factors are involved in elimination of these two groups of sequences.

Production and characterization of a monoclonal antibody for sweat-specific protein and its application for sweat identification

2003 ◽  
Vol 117 (2) ◽  
pp. 90-95 ◽  
Author(s):  
Kazunori Sagawa ◽  
Akihiko Kimura ◽  
Yoshifumi Saito ◽  
Hiroshi Inoue ◽  
Seiji Yasuda ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Specific Protein

scholarly journals Anti-Stress, Glial- and Neuro-Differentiation Potential of Resveratrol: Characterization by Cellular, Biochemical and Imaging Assays

Nutrients ◽  
2020 ◽  
Vol 12 (3) ◽  
pp. 671
Author(s):  
Sajal Afzal ◽  
Sukant Garg ◽  
Divya Adiga ◽  
Yoshiyuki Ishida ◽  
Keiji Terao ◽  
...  
Keyword(s):  
Oxidative Dna Damage ◽  
Specific Protein ◽  
New Drugs ◽  
Protein Markers ◽  
Human Neuroblastoma ◽  
Differentiation Potential ◽  
Daily Lives ◽  
Rat Glioma ◽  
Age Related

Environmental stress, exhaustive industrialization and the use of chemicals in our daily lives contribute to increasing incidence of cancer and other pathologies. Although the cancer treatment has revolutionized in last 2–3 decades, shortcomings such as (i) extremely high cost of treatment, (ii) poor availability of drugs, (iii) severe side effects and (iv) emergence of drug resistance have prioritized the need of developing alternate natural, economic and welfare (NEW) therapeutics reagents. Identification and characterization of such anti-stress NEW drugs that not only limit the growth of cancer cells but also reprogram them to perform their specific functions are highly desired. We recruited rat glioma- and human neuroblastoma-based assays to explore such activities of resveratrol, a naturally occurring stilbenoid. We demonstrate that nontoxic doses of resveratrol protect cells against a variety of stresses that are largely involved in age-related brain pathologies. These included oxidative, DNA damage, metal toxicity, heat, hypoxia, and protein aggregation stresses. Furthermore, it caused differentiation of cells to functional astrocytes and neurons as characterized by the upregulation of their specific protein markers. These findings endorse multiple bioactivities of resveratrol and encourage them to be tested for their benefits in animal models and humans.

scholarly journals Fast-acting and nearly gratuitous induction of gene expression and protein depletion inSaccharomyces cerevisiae

2011 ◽  
Vol 22 (22) ◽  
pp. 4447-4459 ◽  
Author(s):  
R. Scott McIsaac ◽  
Sanford J. Silverman ◽  
Megan N. McClean ◽  
Patrick A. Gibney ◽  
Joanna Macinskas ◽  
...  
Keyword(s):  
Regulatory Networks ◽  
Transcriptional Activator ◽  
Specific Protein ◽  
Yeast Saccharomyces Cerevisiae ◽  
Functional Relationships ◽  
Genome Wide ◽  
Specific Induction ◽  
Specific Degradation ◽  
Fast Acting

We describe the development and characterization of a system that allows the rapid and specific induction of individual genes in the yeast Saccharomyces cerevisiae without changes in nutrients or temperature. The system is based on the chimeric transcriptional activator Gal4dbd.ER.VP16 (GEV). Upon addition of the hormone β-estradiol, cytoplasmic GEV localizes to the nucleus and binds to promoters containing Gal4p consensus binding sequences to activate transcription. With galactokinase Gal1p and transcriptional activator Gal4p absent, the system is fast-acting, resulting in readily detectable transcription within 5 min after addition of the inducer. β-Estradiol is nearly a gratuitous inducer, as indicated by genome-wide profiling that shows unintended induction (by GEV) of only a few dozen genes. Response to inducer is graded: intermediate concentrations of inducer result in production of intermediate levels of product protein in all cells. We present data illustrating several applications of this system, including a modification of the regulated degron method, which allows rapid and specific degradation of a specific protein upon addition of β-estradiol. These gene induction and protein degradation systems provide important tools for studying the dynamics and functional relationships of genes and their respective regulatory networks.

scholarly journals Characterization of the gene for mp20: a Drosophila muscle protein that is not found in asynchronous oscillatory flight muscle.

1989 ◽  
Vol 108 (2) ◽  
pp. 521-531 ◽  
Author(s):  
A Ayme-Southgate ◽  
P Lasko ◽  
C French ◽  
M L Pardue
Keyword(s):  
Calcium Binding ◽  
Muscle Protein ◽  
Primary Cultures ◽  
Specific Protein ◽  
Gene Encoding ◽  
Significant Similarity ◽  
Coding Regions ◽  
Flight Muscles ◽  
Calcium Binding Sites

A Drosophila melanogaster gene encoding a muscle specific protein was isolated by differential screening with RNA from primary cultures of myotubes. The gene encodes a 20-kD protein, muscle protein 20 (mp20), that is not detected in the asynchronous oscillatory flight muscles, but is found in most, if not all, other muscles (the synchronous muscles). The sequence of the protein, deduced from the DNA, contains two regions of 12 amino acids with significant similarity to high-affinity calcium-binding sites of other proteins. This protein is easily extracted from the contractile apparatus and thus does not seem to be a tightly bound structural component. The gene (located in polytene region 49F 9-13) is unique in the D. melanogaster genome and yields two transcripts, 1.0 and 0.9 kb long. The levels of the two transcripts are regulated differently during development, yet the coding regions of the two transcripts are identical.

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