Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.7.49 (reverse transcriptase)
 31,746 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The indole-diterpene paxilline is a potent tremorgenic mammalian mycotoxin and a known inhibitor of maxi-K ion channels. The gene cluster responsible for paxilline biosynthesis in Penicillium paxilli was identified by mapping four large plasmid-induced chromosome deletions. The cluster is predicted to lie within a 50 kb region of chromosome Va and to contain 17 genes, including a geranylgeranyl pyrophosphate (GGPP) synthase (paxG), two FAD-dependent monooxygenases (paxM and N), two cytochrome P450 monooxygenases (paxP and Q), a dimethylallyltryptophan (DMAT) synthase (paxD) and two possible transcription factors (paxR and paxS), which contain a Zn(II)2Cys6 DNA-binding motif. Targeted replacement of paxG confirmed that it is essential for paxilline biosynthesis but dispensable for growth. The GGPP for primary metabolism is predicted to be provided by a second GGPP synthase (ggs1) that was cloned, sequenced and mapped to chromosome IV. Semi-quantitative reverse transcriptase-polymerase chain reaction analysis demonstrated that the expression of paxG, paxM and paxP in submerged liquid cultures of P. paxilli increased dramatically with the onset of paxilline biosynthesis. In contrast, the expression of beta-tubulin (tub2) and ggs1 was not induced. This is the first description of the molecular cloning and genetic analysis of an indole-diterpene gene cluster.
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PMID:Molecular cloning and genetic analysis of an indole-diterpene gene cluster from Penicillium paxilli. 1116 15

We report here two atypical cases of X-linked CGD patients (first cousins) in which cytochrome b(558) is present at a normal level but is not functional (X91+). The mutations were localized by single-strand conformational polymorphism of reverse transcriptase-polymerase chain reaction amplified fragments and then identified by sequence analysis. They consisted in two base substitutions (C919 to A and C923 to G), changing His303 to Asn and Pro304 to Arg in the cytosolic gp91phox C-terminal tail. Mismatched polymerase chain reaction and genomic DNA sequencing showed that mothers had both wild-type and mutated alleles, confirming that this case was transmitted in an X-linked fashion. A normal amount of FAD was found in neutrophil membranes, both in the X91+ patients and their parents. Epstein-Barr virus-transformed B lymphocytes from the X91+ patients acidified normally upon stimulation with arachidonic acid, indicating that the mutated gp91phox still functioned as a proton channel. A cell-free translocation assay demonstrated that the association of the cytosolic factors p47phox and p67phox with the membrane fraction was strongly disrupted. We concluded that residues 303 and 304 are crucial for the stable assembly of the NADPH oxidase complex and for electron transfer, but not for its proton channel activity.
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PMID:Molecular and functional characterization of a new X-linked chronic granulomatous disease variant (X91+) case with a double missense mutation in the cytosolic gp91phox C-terminal tail. 1199 83

Aldehyde oxidase (AO, EC 1.2.3.1) is a molybdenohydroxylase that is considered to catalyze the last step of abscisic acid (ABA) and indole-3-acetic acid (IAA) synthesis. Three cDNAs encoding aldehyde oxidase proteins in Pisum sativum (cv. Little Marvel) were obtained based on RT-PCR (reverse transcriptase-polymerase chain reaction) strategy. The cloned genes, designated as PsAO1, PsAO2 and PsAO3, are 4630, 4347, 4600 bp in length, respectively, and show high sequence identity to each other and to aldehyde oxidases from other plant species. The deduced PsAO1, PsAO2, and PsAO3 proteins are 1373, 1367, 1367 amino acids in length, respectively, and contain consensus sequences for two iron-sulfur centers, a FAD binding domain, and a molybdenum cofactor (Moco) binding domain. PsAO1 and PsAO2 were mainly expressed in leaves of seedlings and young leaves of adult plants, while the highest PsAO3 transcript level was observed in aging leaves and matured seeds. PsAO2 mRNA was not affected by salinity or ammonium treatment, whereas the transcript level of PsAO3 increased significantly under both stress conditions, with the most pronounced changes in aging leaves, fully expanded leaves and roots. The PsAO1 transcript level was enhanced only in the presence of ammonium in the nutrient medium, but not under salinity. Based on the molecular mass of the deduced proteins and on organ-specific gene expression, studied both under control and stress conditions, the contribution of each PsAO cDNA in the formation of the previously described three dimeric pea AO isoforms and the possible involvement of the PsAO3 in abscisic acid (ABA) synthesis is discussed.
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PMID:Molecular cloning, characterization and expression analysis of three aldehyde oxidase genes from Pisum sativum L. 1800 24

Nitric oxide (NO) signaling is involved in many physiological processes in vertebrates and invertebrates. In crustaceans, nitric oxide synthase (NOS) plays a significant role in the regulation of the nervous system and in innate immunity. Here, we describe the entire cDNA sequence (4616 bp) of the kuruma shrimp Marsupenaeus japonicus NOS (Mj NOS) generated using the reverse transcriptase-polymerase chain reaction (RT-PCR) and 5'- and 3'- rapid amplification PCRs of cDNA ends from brain and gill mRNAs. The open reading frame of Mj NOS encoded a protein of 1187 amino acids with an estimated mass of 134 kDa, and had an 82.3% sequence homology with the NOS gene of the land crab Gecarcinus lateralis. Highly conserved amino acid sequences in heme and tetrahydrobiopterin were observed in the oxygenase domain. FMN, FAD and NADPH were found in the reductase domain. Mj NOS mRNA was constitutively expressed in the brain, gill, intestine, thoracic ganglion and testis of the kuruma shrimp. When Vibrio penaeicida was injected into the kuruma shrimp, Mj NOS was expressed in the brain, gill, heart, lymphoid organ, intestine and thoracic ganglion. Mj NOS expression in the gill reached its peak 12 h and decreased to its normal level 24 h after V. penaeicida injection.
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PMID:Molecular cloning and characterization of the nitric oxide synthase gene from kuruma shrimp, Marsupenaeus japonicus. 2010 58