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Growing Family (growing + family)
Selected AbstractsKi-1/57 interacts with PRMT1 and is a substrate for arginine methylationFEBS JOURNAL, Issue 17 2006Dario O. Passos The human 57 kDa Ki-1 antigen (Ki-1/57) is a cytoplasmic and nuclear protein, associated with Ser/Thr protein kinase activity, and phosphorylated at the serine and threonine residues upon cellular activation. We have shown that Ki-1/57 interacts with chromo-helicase DNA-binding domain protein 3 and with the adaptor/signaling protein receptor of activated kinase 1 in the nucleus. Among the identified proteins that interacted with Ki-1/57 in a yeast two-hybrid system was the protein arginine-methyltransferase-1 (PRMT1). Most interestingly, when PRMT1 was used as bait in a yeast two-hybrid system we were able to identify Ki-1/57 as prey among 14 other interacting proteins, the majority of which are involved in RNA metabolism or in the regulation of transcription. We found that Ki-1/57 and its putative paralog CGI-55 have two conserved Gly/Arg-rich motif clusters (RGG/RXR box, where X is any amino acid) that may be substrates for arginine-methylation by PRMT1. We observed that all Ki-1/57 protein fragments containing RGG/RXR box clusters interact with PRMT1 and are targets for methylation in vitro. Furthermore, we found that Ki-1/57 is a target for methylation in vivo. Using immunofluorescence experiments we observed that treatment of HeLa cells with an inhibitor of methylation, adenosine-2,,3,-dialdehyde (Adox), led to a reduction in the cytoplasmic immunostaining of Ki-1/57, whereas its paralog CGI-55 was partially redistributed from the nucleus to the cytoplasm upon Adox treatment. In summary, our data show that the yeast two-hybrid assay is an effective system for identifying novel PRMT arginine-methylation substrates and may be successfully applied to other members of the growing family of PRMTs. [source] Role of Bcl-2 family of proteins in malignancyHEMATOLOGICAL ONCOLOGY, Issue 2 2002Belinda C. Baliga Abstract B cell lymphoma gene-2 (Bcl-2) is the prototypic member of a growing family of proteins that play evolutionarily conserved, key regulatory roles in apoptosis. The Bcl-2 family members are characterized by the presence of one or more Bcl-2 homology domains and are comprised of both the prosurvival and proapoptotic proteins. Bcl-2 itself is a prosurvival member of the family and its aberrant expression has been linked to a variety of different cancers, including several hematological malignancies. Although the exact mechanism of action of Bcl-2 family of proteins in regulating apoptosis is still a matter of some debate, these proteins appear to act upstream of caspase activation. Many recent studies have shown the therapeutic potential of targeting Bcl-2 family members for the treatment of cancer. This article summarizes what is currently known about Bcl-2-like proteins and how the evolving understanding of the biology of these proteins is paving way for the development of novel cancer therapeutics. Copyright © 2001 John Wiley & Sons, Ltd. [source] Transmembrane adapters: attractants for cytoplasmic effectorsIMMUNOLOGICAL REVIEWS, Issue 1 2003Jonathan A. Lindquist Summary: Transmembrane adapter proteins (TRAPs) are a relatively new and growing family of proteins that include linker for activation of T cells (LAT), phosphoprotein associated with glycosphingolipid-enriched micro domains (PAG)/C-terminal Src kinase (Csk) binding protein (Cbp), SHP2-interacting transmembrane adapter protein (SIT), T cell receptor interacting molecule (TRIM), and the recently identified non-T cell activation linker (NTAL) and pp30. TRAPs share several common structural features, but more importantly they possess multiple sites of tyrosine phosphorylation, by which they act as scaffolds for recruiting cytosolic adapter and/or effector proteins. The membrane association of TRAPs places them near to the immunoreceptors, a position from which they coordinate and modulate the signals they receive to produce an appropriate cellular response. [source] Proteinaceous inhibitors of carbohydrate-active enzymes in cereals: implication in agriculture, cereal processing and nutrition,JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, Issue 11 2006Nathalie Juge Abstract Enzymes that degrade, modify, or create glycosidic bonds are involved in carbohydrate biosynthesis and remodelling. Microbial carbohydrate-active enzymes form the basis of current green technology in the food, feed, starch, paper and pulp industries and the revolution in genomics may offer long-term gains on the quality and quantity of the raw materials. Proteinaceous inhibitors of carbohydrate-active enzymes (,-amylase, limit-dextrinase, polygalacturonase, pectin lyase, pectin methylesterase, invertase and xyloglucan endoglucanase) naturally occur in plants where they are involved in various roles from plant defence to metabolism. Xylanase inhibitors represent the latest addition to this growing family. In this review, we will focus on the inhibitors of carbohydrate-active enzymes present in cereals, mostly represented by ,-amylase and xylanase inhibitors, and summarise the existing knowledge on their structure, function, and implication in cereal processing, agriculture and nutrition. Copyright © 2006 Society of Chemical Industry [source] The Nep1-like proteins,a growing family of microbial elicitors of plant necrosisMOLECULAR PLANT PATHOLOGY, Issue 4 2004CLARE L. PEMBERTON SUMMARY A novel family of microbial elicitors of plant necrosis has been identified. Designated Nep1-like proteins (NLPs), after the first family member isolated, they range from 24 to 26 kDa and are found in a variety of taxonomically unrelated micro-organisms. These include several fungi and oomycetes, as well as Gram-positive and Gram-negative bacteria. Some NLPs induce a hypersensitive-like response in plants, although the basis for initiation of this response remains unclear. Similarly, the cellular role of such highly conserved proteins is undetermined. It is not clear whether the NLPs are dedicated elicitors of plant defences or whether this induction occurs as a result of another activity. [source] New vanadium(IV) and titanium(IV) oxyfluorotellurates(IV): V2Te2O7F2 and TiTeO3F2ACTA CRYSTALLOGRAPHICA SECTION C, Issue 1 2009Jean Paul Laval As part of a continuing study of oxyfluorotellurates(IV), materials likely to present interesting nonlinear optical properties, two new phases, titanium(IV) tellurium(IV) trioxide difluoride, TiTeO3F2, and divanadium(IV) ditellurium(IV) heptaoxide difluoride, V2Te2O7F2, have been characterized and present, respectively, titanium and vanadium in the tetravalent state. The TiTeO3F2 structure is based on linear double rows of TiO3F3 polyhedra sharing vertices. These rows are connected to adjacent rows via two vertices of Te2O5 bipolyhedra. The Te, Ti, one F and two O atoms are on general positions, with one O and F statistically occupying the same site with half-occupancy for each anion. One O and one F occupy sites with .m. symmetry. The V2Te2O7F2 structure consists of zigzag chains of VO4F2 octahedra alternately sharing O,O and F,F edges. These chains are connected via Te2O5 bipolyhedra, forming independent mixed layers. The Te, V, one F and three O atoms are on general positions while one O atom occupies a site of symmetry. In both phases, the electronic lone pair E of the TeIV atom is stereochemically active. A full O/F anionic ordering is observed in V2Te2O7F2, but in TiTeO3F2 one of the six anionic sites is occupied by half oxygen and half fluorine, all the others being strictly ordered. These compounds represent new members of a growing family of oxyfluorotellurates(IV), including the recently characterized members of formula MTeO3F, M being a trivalent cation. As was true for the previous members, they are characterized by an unusually high thermal and chemical stability in relation to the absence of direct Te,F bonds. [source] Structure of pteridine reductase (PTR1) from Leishmania tarentolaeACTA CRYSTALLOGRAPHICA SECTION D, Issue 9 2003Haiyan Zhao The protozoan parasites Leishmania utilize a pteridine-reducing enzyme, pteridine reductase (PTR1), to bypass antifolate inhibition. The crystal structure of PTR1 from L. tarentolae has been solved as a binary complex with NADPH at 2.8,Å resolution. The structure was solved by molecular-replacement techniques using the recently reported L. major PTR1 structure as a search model. Comparisons of the present structure with the L. major PTR1 allowed us to identify regions of flexibility in the molecule. PTR1 is a member of the growing family of short-chain dehydrogenases (SDR) which share the characteristic Tyr(Xaa)3Lys motif in the vicinity of the active site. The functional enzyme is a tetramer and the crystallographic asymmetric unit contains a tetramer with 222 point-group symmetry. [source] Electrophysiological Characteristics Of The Ca2+ -Activated Cl, Channel Family Of Anion Transport ProteinsCLINICAL AND EXPERIMENTAL PHARMACOLOGY AND PHYSIOLOGY, Issue 11 2000Catherine M Fuller SUMMARY 1. A protein isolated from the bovine tracheal epithelium behaves as a Ca2+ -activated Cl, channel (CaCC) when incorporated into planar lipid bilayers. 2. An antibody raised against this protein was used to screen a cDNA expression library and resulted in the isolation of a cDNA clone that exhibited nearly identical electrophysiological characteristics to the isolated endogenous protein when expressed. 3. Recent cloning of several related proteins has revealed that the cloned bovine CaCC is one of a large and growing family. All new family members so far examined are associated with the appearance of a novel Ca2+ -mediated Cl, conductance when heterologously expressed. 4. This new group of proteins may underlie the Ca2+ -mediated Cl, conductance upregulated in the cystic fibrosis (CF) knockout mouse and thought to be responsible for the escape from the significant airway pathology associated with CF. [source] | |||||||||||||