Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Colin Hanfrey"'
Publikováno v:
The Journal of Biological Chemistry
Polyamines are fundamental molecules of life, and their deep evolutionary history is reflected in extensive biosynthetic diversification. The polyamines putrescine, agmatine, and cadaverine are produced by pyridoxal 5′-phosphate-dependent L-ornithi
Autor:
Steven E. Ealick, Anthony J. Michael, Yang Zhang, Bin Li, Katherine A. Elliott, Colin Hanfrey, Sok Ho Kim
Publikováno v:
Molecular Microbiology. 97:791-807
The polyamine spermidine is absolutely required for growth and cell proliferation in eukaryotes, due to its role in post-translational modification of essential translation elongation factor eIF5A, mediated by deoxyhypusine synthase. We have found th
Publikováno v:
Molecular Microbiology. 86:485-499
Summary Structural backbones of iron-scavenging siderophore molecules include polyamines 1,3-diaminopropane and 1,5-diaminopentane (cadaverine). For the cadaverine-based desferroxiamine E siderophore in Streptomyces coelicolor, the corresponding bios
Autor:
Margaret A. Phillips, Duncan J. H. Gaskin, Colin Hanfrey, Jeongmi Lee, Patrick M. Woster, Stuart T. Hazeldine, Bruce M. Pearson, Anthony J. Michael
Publikováno v:
Journal of Biological Chemistry. 286:43301-43312
The availability of fully sequenced bacterial genomes has revealed that many species known to synthesize the polyamine spermidine lack the spermidine biosynthetic enzymes S-adenosylmethionine decarboxylase and spermidine synthase. We found that such
Autor:
Anthony J. Michael, Robert T. Green, Colin Hanfrey, Anthony E. Pegg, Xiaojing Wang, Sreenivas Kanugula, Katherine A. Elliott, Diane E. McCloskey
Publikováno v:
Molecular Microbiology. 81:1109-1124
Summary We have identified gene fusions of polyamine biosynthetic enzymes S-adenosylmethionine decarboxylase (AdoMetDC, speD) and aminopropyltransferase (speE) orthologues in diverse bacterial phyla. Both domains are functionally active and we demons
Publikováno v:
FEBS Letters. 582:503-509
Accumulation of unfolded proteins in the endoplasmic reticulum (ER) causes stress and induces the unfolded protein response (UPR). Genome-wide analysis of translational regulation in response to the UPR-inducing agent dithiothreitol in Saccharomyces
Autor:
Anthony J. Michael, Colin Hanfrey, Katherine A. Elliott, Marina Franceschetti, Crista Illingworth, Melinda J. Mayer
Publikováno v:
Journal of Biological Chemistry. 280:39229-39237
A novel form of translational regulation is described for the key polyamine biosynthetic enzyme S-adenosylmethionine decarboxylase (AdoMetDC). Plant AdoMetDC mRNA 5' leaders contain two highly conserved overlapping upstream open reading frames (uORFs
Autor:
M. Collier, Barry Perry, Anthony J. Michael, Crista Illingworth, Katherine A. Elliott, Colin Hanfrey, Marina Franceschetti, Melinda J. Mayer, B. Thompson
Publikováno v:
Biochemical Society Transactions. 31:424-427
It is becoming apparent that control of protein synthesis by metabolites is more common than previously thought. Much of that control is exerted at the level of initiation of mRNA translation, orchestrated by upstream open reading frames (uORFs) and
Publikováno v:
The Plant Journal. 27:551-560
Unlike other eukaryotes, which can synthesize polyamines only from ornithine, plants possess an additional pathway from arginine. Occasionally non-enzymatic decarboxylation of ornithine could be detected in Arabidopsis extracts; however, we could not
Autor:
Marina FRANCESCHETTI, Colin HANFREY, Sonia SCARAMAGLI, Patrizia TORRIGIANI, Nello BAGNI, Daniel BURTIN, Anthony J. MICHAEL
Publikováno v:
Biochemical Journal. 353:403-409
S-Adenosyl-L-methionine decarboxylase (AdoMetDC; EC 4.1.1.50) is one of the key regulatory enzymes in the biosynthesis of polyamines. Isolation of genomic and cDNA sequences from rice and Arabidopsis had indicated that this enzyme is encoded by a sma