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.

scholarly journals Mutations in calphotin, the gene encoding a Drosophila photoreceptor cell-specific calcium-binding protein, reveal roles in cellular morphogenesis and survival.

Genetics ◽  
1994 ◽  
Vol 138 (2) ◽  
pp. 413-421 ◽  
Author(s):  
Y Yang ◽  
D Ballinger
Keyword(s):  
Calcium Binding ◽  
Photoreceptor Cell ◽  
Cell Structure ◽  
Specific Protein ◽  
Cell Organelle ◽  
Cell Type ◽  
Gene Encoding ◽  
Cellular Morphogenesis ◽  
Transgenic Flies ◽  
Drosophila Photoreceptor

Abstract Calphotin is a Drosophila photoreceptor cell-specific protein expressed very early in eye development, at the time when cell-type decisions are being made. Calphotin is a very hydrophobic and proline-rich protein which lacks obvious transmembrane domains. The cDNA encoding Calphotin was mapped to a region removed by a set of existing chromosomal deletions. Mutations that alter photoreceptor cell structure and development were isolated that fail to complement these deletions. These mutations fall into two classes. Class I mutations alter the structure of the rhabdomere, a photoreceptor cell organelle specialized for phototransduction. Class II mutations have rough eyes, due to misorientation of the rhabdomeres and photoreceptor cell death. Transformation rescue of these phenotypes in transgenic flies bearing calphotin genomic DNA indicates that both classes of mutations are in the calphotin gene. Analysis of these mutations suggest that Calphotin plays important roles in both rhabdomere development and in photoreceptor cell survival.

scholarly journals Characterization of the calcium-binding sites of calcineurin B

FEBS Letters ◽  
1995 ◽  
Vol 362 (1) ◽  
pp. 55-58 ◽  
Author(s):  
Lazaros T Kakalis ◽  
Michael Kennedy ◽  
Robert Sikkink ◽  
Frank Rusnak ◽  
Ian M Armitage
Keyword(s):  
Binding Sites ◽  
Calcium Binding ◽  
Calcineurin B ◽  
Calcium Binding Sites

scholarly journals Isolation and Characterization of the First Temperate Virus Infecting Psychrobacillus from Marine Sediments

Viruses ◽  
2022 ◽  
Vol 14 (1) ◽  
pp. 108
Author(s):  
Wang Liu ◽  
Xiaowei Zheng ◽  
Xin Dai ◽  
Zhenfeng Zhang ◽  
Wenyan Zhang ◽  
...  
Keyword(s):  
Marine Sediments ◽  
Hydrothermal Vent ◽  
Okinawa Trough ◽  
Marine Ecosystem ◽  
Genome Replication ◽  
Gene Encoding ◽  
Significant Similarity ◽  
Host Chromosome ◽  
Isolation And Characterization

Viruses are far more abundant than cellular microorganisms in the marine ecosystem. However, very few viruses have so far been isolated from marine sediments, especially hydrothermal vent sediments, hindering the understanding of the biology and ecological functions of these tiny organisms. Here, we report the isolation and characterization of a temperate bacteriophage, named PVJ1, which infects Psychrobacillus from a hydrothermal vent field in Okinawa Trough. PVJ1 belongs to the Myoviridae family of the order Caudovirales. The tailed phage possesses a 53,187 bp linear dsDNA genome, with 84 ORFs encoding structural proteins, genome replication, host lysis, etc. in a modular pattern. The phage genome is integrated into the host chromosome near the 3′-end of deoD, a gene encoding purine nucleoside phosphorylase (PNP). The phage integration does not appear to disrupt the function of PNP. The phage DNA is packaged by the headful mechanism. Release of PVJ1 from the host cell was drastically enhanced by treatment with mitomycin C. Phages encoding an MCP sharing significant similarity (≥70% identical amino acids) with that of PVJ1 are widespread in diverse environments, including marine and freshwater sediments, soils, artificial ecosystems, and animal intestines, and primarily infect Firmicutes. These results are valuable to the understanding of the lifestyle and host interactions of bacterial viruses at the bottom of the ocean.

scholarly journals Characterization of Two Distinct Calcium-Binding Sites in the Amino-Terminus of Human Profilaggrin

1995 ◽  
Vol 104 (2) ◽  
pp. 218-223 ◽  
Author(s):  
Richard B. Presland ◽  
James A. Bassuk ◽  
Janet K. Kimball ◽  
Beverly A. Dale
Keyword(s):  
Binding Sites ◽  
Calcium Binding ◽  
Amino Terminus ◽  
Calcium Binding Sites

Cloning and characterization of an immunoreactive gene encoding a calcium-binding protein from Naegleria fowleri

2004 ◽  
Vol 137 (1) ◽  
pp. 169-173 ◽  
Author(s):  
Seok-Ryoul Jeong ◽  
Myung-Soo Cho ◽  
Sun Park ◽  
Kyongmin Hwang Kim ◽  
Kyoung-Ju Song ◽  
...  
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Naegleria Fowleri ◽  
Gene Encoding ◽  
Nægleria Fowleri

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.

Cloning and characterization of MdGST1 from red apple leaves

2018 ◽  
Vol 98 (5) ◽  
pp. 1150-1158
Author(s):  
Xiaolei Han ◽  
Caixia Zhang ◽  
Yi Tian ◽  
Hera Gul ◽  
Peihua Cong ◽  
...  
Keyword(s):  
Anthocyanin Biosynthesis ◽  
Transcript Level ◽  
Glutathione S Transferase ◽  
Gene Encoding ◽  
Protein Coding ◽  
Apple Variety ◽  
Coding Regions ◽  
Qrt Pcr ◽  
Rapid Amplification

Glutathione S-transferase (GST) is involved in the downstream steps of the anthocyanin biosynthesis pathway in plants. However, the gene(s) encoding this enzyme have not been isolated from apple (Malus × domestica Borkh.) yet. We isolated a gene encoding GST from leaves of the red-fleshed apple variety ‘Royalty’ by full cDNA library sequencing and the 3′ rapid-amplification of cDNA ends method, and designated it MdGST1. In total, seven different MdGST1 transcripts were found. These had three different untranslated but identical protein-coding regions. Phylogenetic analysis showed that MdGST1 is a TT19-type GST, which is involved in anthocyanin transport. qRT-PCR analyses showed that the transcript level of MdGST1 was much higher in red leaves than in bagged or green leaves. When MdGST1 was introduced into a non-pigmented mutant of Arabidopsis, the transformants showed a visible purple phenotype in leaves and stems. Our results suggest that MdGST1 plays a role in anthocyanin biosynthesis. This information will help to improve the understanding of the mechanism of apple coloration.

scholarly journals Characterization of two novel EF-hand proteins identifies a clade of putative Ca2+-binding protein specific to the Ambulacraria

2020 ◽  
Author(s):  
Arisnel Soto-Acabá ◽  
Pablo A. Ortíz-Pineda ◽  
José E. García-Arrarás
Keyword(s):  
Calcium Binding ◽  
Phylogenetic Analyses ◽  
Sequence Alignments ◽  
Multiple Sequence ◽  
Significant Similarity ◽  
Significant Differential Expression ◽  
Multiple Sequence Alignments ◽  
Ef Hand ◽  
Protein Discovery

AbstractIn recent years, transcriptomic databases have become one of the main sources for protein discovery. In our studies of nervous system and digestive tract regeneration in echinoderms, we have identified several transcripts that have attracted our attention. One of these molecules corresponds to a previously unidentified transcript (Orpin) from the sea cucumber Holothuria glaberrima that appeared to be upregulated during intestinal regeneration. We have now identified a second highly similar sequence and analyzed the predicted proteins using bioinformatics tools. Both sequences have EF-hand motifs characteristic of calcium-binding proteins (CaBPs) and N-terminal signal peptides. Sequence comparison analyses such as multiple sequence alignments and phylogenetic analyses only showed significant similarity to sequences from other echinoderms or from hemichordates. Semi-quantitative RT-PCR analyses revealed that transcripts from these sequences are expressed in various tissues including muscle, haemal system, gonads, and mesentery. However, contrary to previous reports, there was no significant differential expression in regenerating tissues. Nonetheless, the identification of unique features in the predicted proteins suggests that these might comprise a novel subfamily of EF-hand containing proteins specific to the Ambulacraria clade.

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