PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 11089217

Analyzing reverse gyrase activity.

M Duguet·C Jaxel·A C Déclais·F Confalonieri·J Marsault·C Bouthier de la Tour·M Nadal·C Portemer
View original source ↗Export metadata ↓

Abstract

The source did not provide an abstract. Follow the original record for more information.

Explore related subjects

Adenosine TriphosphatasesAdenosine TriphosphateArchaeaBacteriaCatalysisDNA Topoisomerases, Type IDNA Topoisomerases, Type IIDNA, CircularDNA, SuperhelicalElectrophoresis, Agar GelNucleic Acid ConformationNucleic Acid DenaturationPolyethylene GlycolsProtein Structure, TertiaryJournal ArticleResearch Support, Non-U.S. Gov't

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

M Duguet, C Jaxel, A C Déclais, F Confalonieri, J Marsault, C Bouthier de la Tour, M Nadal, C Portemer. 2001. Analyzing reverse gyrase activity.. https://doi.org/10.1385/1-59259-057-8%3A35

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2008

Isolation and characterization of Plasmodium falciparum UAP56 homolog: evidence for the coupling of RNA binding and splicing activity by site-directed mutations.

UAP56 (U2AF65 associated protein) is a member of the DEAD-box helicase family. Helicases are essential enzymes generally involved in the metabolism of nucleic acids. The gene encoding a member of DEAD-box family was cloned and characterized from the human malaria parasite Plasmodium falciparum. PfU52 is homologous to UAP56 and contains the RNA-dependent ATPase, RNA helicase and RNA binding activities. Using the parasite extract we report that PfU52 is involved in splicing reaction. Site-directed mutagenesis studies indicate that the conserved residues glycine 181, isoleucine 182 and arginine 206 are involved in RNA binding and this activity is required for the enzymatic activities of PfU52. PfU52 is expressed in all the intraerythrocytic developmental stages of the parasite. In the present study we have reported the detailed characterization of PfU52 from P. falciparum and these results advance the knowledge regarding the function of UAP56 in general.

Adenosine Triphosphatases↗
PubMed2001

The betam protein, a member of the X,K-ATPase beta-subunits family, is located intracellularly in pig skeletal muscle.

The sequence of the pig cDNA encoding the muscle-specific betam-protein, a member of the X,K-ATPase beta-subunits family, was determined. Two alternatively spliced transcripts encoding polypeptide chains of 355 and 351 residues were identified. The tissue specificity of expression of betam and other X,K-ATPase beta-subunit genes was studied by RT-PCR performed on 24 tissues from newborn pigs. The betam expression was shown to be highly tissue-specific, being detected at the highest level in skeletal muscle, at a lower level in heart, and at much lower level in skin. The betam transcripts are more abundant in the tissues from the newborn than adult. Immunoblotting and deglycosylation shift assay indicated that skeletal muscle membranes of newborn pigs contain betam protein with an electrophoretic mobility and carbohydrate content very similar to that of human betam. Fractionation of membranes from both newborn and adult pig skeletal muscles by isopycnic centrifugation revealed that the majority of the betam protein is concentrated in the sarcoplasmic reticulum-containing fractions. This intracellular location is a unique property that distinguishes the betam protein from other members of the X,K-ATPase beta-subunit family.

Adenosine Triphosphatases↗
PubMed2001

Molecular cloning and characterization of the Cl(-) pump-associated 55-kDa protein in rat brain.

The Cl(-)-ATPase/pump in the plasma membrane of the rat brain is a candidate for active outwardly directed Cl(-) translocating systems. We recently isolated a Cl(-) pump, 520- or 580-kDa protein complex, which consisted of 51-, 55-, 60-, and 62-kDa proteins. In this study, we cloned a cDNA encoding a 55-kDa glycoprotein, designated as ClP55, which contained an open reading frame of 1512 base pairs encoding a protein of 504 amino acids including a signal peptide of 28 amino acids. Northern and Western blot analyses demonstrated expression of ClP55 mainly in the cerebrum. Application of antisense phosphorothioate oligonucleotides to cultured neurons resulted in a marked increase in the intracellular Cl(-) concentration ([Cl(-)](i)). Immunohistochemical analysis indicated that ClP55 was localized to the plasma membranes of neurons such as hippocampal pyramidal neurons and cerebellar Purkinje cells. Taken together, these results suggest that ClP55 is one of the Cl(-) pump subunits responsible for Cl(-) pump activity.

Adenosine Triphosphatases↗