Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.30.1 (S1 nuclease)
 3,660 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Egasyn (esterase-22), a member of the nonspecific carboxylesterase multigene family (E.C. 3.1.1.1), is the endoplasmic reticulum (ER)-targeting protein of beta-glucuronidase. We utilized the polymerase chain reaction (PCR) in the eventual isolation of murine egasyn cDNAs. PCR primers were based upon: (1) partial amino acid sequences derived from egasyn peptides and (2) a conserved active site region shared by carboxylesterases. The amino acid sequence deduced from the PCR product matched that obtained from egasyn protein. This product was utilized as a probe to screen a cDNA library. Two cDNAs whose composite sequence encoded an open reading frame of 562 amino acids were isolated. A message size of 1700-2000 bp was revealed by RNA blot hybridization analysis. S1 nuclease protection analyses detected mRNA in liver, kidney, lung, and submandibular gland, but not in spleen, brain, and testes. Genetic mapping confirmed the location of an egasyn cDNA fragment in cluster 1 of the esterase region on chromosome 8. Transfection of COS cells with the 2022-bp cDNA resulted in the expression of esterase activity, which comigrated on native gels with liver esterase-22. The features of the deduced amino acid sequence of the egasyn cDNA are compared with previously characterized carboxylesterases and with other lumenal ER proteins.
 ...
PMID:Characterization and functional expression of a cDNA encoding egasyn (esterase-22): the endoplasmic reticulum-targeting protein of beta-glucuronidase. 178 3

We have characterized a mRNA sequence containing the entire coding region of a mouse carboxylesterase (EC 3.1.1.1). pEs-N, an 1840-bp composite of five overlapping cDNA clones, contains an open reading frame of 554 amino acids that display a high degree of similarity with rat and rabbit carboxylesterases. Genetic mapping studies place this carboxylesterase in cluster 1 of the esterase region on chromosome 8. Results of blot hybridization analysis of genomic DNA probed with a pEs-N cDNA under both low and high stringency conditions suggest membership in a carboxylesterase multigene family, as would be expected for a nonspecific carboxylesterase. A message size of 1850-1900 nucleotides was revealed by RNA blot hybridization analysis. S1 nuclease protection analyses with a probe representing a segment of pEs-N detected message in liver, kidney, and lung, but not in spleen, brain, testes, and submandibular gland, with higher levels in female than in male kidney. Additional S1 nuclease-protected mRNA species were found, suggesting the expression of distinct members of a multigene family. In vitro translation of a full-size transcript of pEs-N resulted in a product of 51.5 kDa. Upon the addition of microsomes, this product was processed into a protein of 60.4 kDa, which is within the size range of monomeric units of mouse carboxylesterases.
 ...
PMID:Characterization of a murine cDNA encoding a member of the carboxylesterase multigene family. 184 May 65

Gradients of gene expression are maintained along the proximal-distal axis of the mammalian small intestine despite a continuously regenerating epithelium. To study the molecular mechanisms responsible for this phenomenon, we utilized a subtractive hybridization strategy to isolate genes differentially expressed in the duodenum but not ileum. We isolated and sequenced 15 clones. The clones were fragments of genes encoding lipases, proteases, and an esterase. A novel clone was characterized and subsequently shown to encode syncollin, a secretory granule protein that binds to syntaxin in a calcium-sensitive manner. RT-PCR and S1 nuclease protection assay were used to clarify the 5'-end of syncollin. Syncollin was expressed in the rat pancreas, spleen, duodenum, and colon. In situ hybridization localized syncollin expression in the pancreas to acinar cells and in the duodenum to villus epithelial cells.
 ...
PMID:Syncollin is differentially expressed in rat proximal small intestine and regulated by feeding behavior. 1066 56

The vernacular name 'fluorescent Pseudomonas group 97-514' was coined for a group of 43 strains isolated from two French natural mineral waters. All these strains were gram-negative, rod-shaped and motile by means of a single polar flagellum. They produced fluorescent pigment (pyoverdin) on King B medium, catalase and cytochrome oxidase. They were capable of respiratory but not fermentative metabolism. They were not able to accumulate poly-beta-hydroxybutyrate and possessed an arginine dihydrolase system. DNA-DNA relatedness studies (S1 nuclease method) showed that the 43 strains of 'fluorescent Pseudomonas group 97-514' formed a genetically homogeneous group (DNA-DNA relatedness ranged from 70 to 100%). A total of 76 strains representing well-known or partially characterized species of the genus Pseudomonas sensu stricto had 7-56% DNA hybridization with strain CFML 97-514T. The highest DNA binding values were found with Pseudomonas veronii CIP 104663T (52%), Pseudomonas rhodesiae CIP 104664T (56%), Pseudomonas marginalis ATCC 10844T (56%), Pseudomonas gessardii CIP 105469T (53%) and Pseudomonas cedrella CIP 105541T (52%). Their unrelatedness was confirmed by deltaTm values greater than 7 degrees C. On the basis of the results of phenotypic and DNA-DNA hybridization studies, a novel Pseudomonas species, Pseudomonas grimontii sp. nov., is proposed for the 43 strains of 'fluorescent Pseudomonas group 97-514'. The type strain is strain CFML 97-514T (= CIP 106645T = ATCC BAA-140T). The G+C content of the DNA of the type strain was 58 mol%. A comparison of the complete 16S rRNA gene sequence of the type strain CFML 97-514T and the sequence of other strains of the genus Pseudomonas revealed that the novel species fell within the 'Pseudomonas fluorescens intrageneric cluster'. Members of P. grimontii grew at 4 degrees C but not at 41 degrees C. They were able to use D-xylose, alpha-L-rhamnose, alpha-aminobutyrate, meso-erythritol and itaconate as sole sources of carbon and energy and formed levan from sucrose. Strains do not possess lecithinase or Tween esterase activities. The clinical significance of P. grimontii is unknown.
 ...
PMID:Pseudomonas grimontii sp. nov. 1236 Dec 51