Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Jed H. Doelling"'
Publikováno v:
PLoS ONE, Vol 2, Iss 8, p e815 (2007)
The silencing of one parental set of rRNA genes in a genetic hybrid is an epigenetic phenomenon known as nucleolar dominance. We showed previously that silencing is restricted to the nucleolus organizer regions (NORs), the loci where rRNA genes are t
Externí odkaz:
https://doaj.org/article/1f92ac1fd3034252a4564f1ec5dcb802
Autor:
Jennifer Chandler, Jed H. Doelling, Gulsum Soyler-Ogretim, Jasen Wise, Allison R. Phillips, Richard D. Vierstra, Judy Callis, Marisa S. Otegui
Publikováno v:
Plant Physiology. 145:801-813
Deubiquitinating enzymes are essential to the ubiquitin (Ub)/26S proteasome system where they release Ub monomers from the primary translation products of poly-Ub and Ub extension genes, recycle Ubs from polyubiquitinated proteins, and reverse the ef
Publikováno v:
Plant Physiology. 138:2097-2110
Autophagy is an important mechanism for nonselective intracellular breakdown whereby cytosol and organelles are encapsulated in vesicles, which are then engulfed and digested by lytic vacuoles/lysosomes. In yeast, this encapsulation employs a set of
Autor:
Hyoung Yool Lee, Inhwan Hwang, Stephen B. Ryu, Sung Chul Bahn, Kyoungwhan Back, Jeong Sheop Shin, Jed H. Doelling
Publikováno v:
Progress in Lipid Research. 44:52-67
Multiple secretory phospholipase A2 (sPLA2) genes have been identified in plants and encode isoforms with distinct regulatory and catalytic properties. Elucidation of this genetic and biochemical heterogeneity has provided important clues to the regu
Publikováno v:
Protein Expression and Purification. 34:280-283
The gene coding for APG8a (At4g21980), a protein from Arabidopsis thaliana, is involved in the autophagy process. The protein is an interesting candidate for structure determination by NMR spectroscopy. Toward this end, APG8a fused to an N-terminal H
Publikováno v:
The Plant Journal. 27:393-405
The ubiquitin/26S proteasome pathway is a major route for selectively degrading cytoplasmic and nuclear proteins in eukaryotes. In this pathway, chains of ubiquitins become attached to short-lived proteins, signalling recognition and breakdown of the
Publikováno v:
Plant Physiology. 124:1828-1843
Ubiquitin-specific proteases (UBPs) are a family of unique hydrolases that specifically remove polypeptides covalently linked via peptide or isopeptide bonds to the C-terminal glycine of ubiquitin. UBPs help regulate the ubiquitin/26S proteolytic pat
Autor:
Mark Hochstrasser, Jed H. Doelling, Hongyong Fu, Daniel Finley, Richard D. Vierstra, Steven van Nocker, Pierre Alain Girod
Publikováno v:
Molecular Biology Reports. 26:137-146
As initial steps to define how the 26S proteasome degrades ubiquitinated proteins in plants, we have characterized many of the subunits that comprise the proteolytic complex from Arabidopsis thaliana. A set of 23 Arabidopsis genes encoding the full c
Publikováno v:
The Plant Journal. 7:273-286
In Arabidopsis thaliana ribosomal RNA genes (rRNA genes or rDNA) are grouped in two nucleolus organizer regions(NORs) that together comprise approximately 6% of the genome. The map positions of the NORs relative to other genetic markers are unknown.
Publikováno v:
Proceedings of the National Academy of Sciences. 90:7528-7532
In eukaryotes, RNA polymerase I transcription is controlled by DNA elements located within the spacers that separate the tandemly arranged rRNA genes. Unlike rRNA coding sequences, the intergenic spacers evolve rapidly and have little sequence simila