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Metabolomics,Unknown,Transcriptomics,Genomics,Proteomics

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RNAi knock down in Drosophila of THO2 and HPR1 proteins from S2 cells

ABSTRACT: THO2 and HPR1 proteins were co-depleted from Drosophila S2 cells and their role in mRNA export analysed by comparing total RNA and cytoplasmic RNA

ORGANISM(S): Drosophila melanogaster

SUBMITTER: Jan Rehwinkel

PROVIDER: E-MEXP-88 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha.

Jínek Martin M Rehwinkel Jan J Lazarus Brooke D BD Izaurralde Elisa E Hanover John A JA Conti Elena E

Nature structural & molecular biology 20040912 10

Addition of N-acetylglucosamine (GlcNAc) is a ubiquitous form of intracellular glycosylation catalyzed by the conserved O-linked GlcNAc transferase (OGT). OGT contains an N-terminal domain of tetratricopeptide (TPR) repeats that mediates the recognition of a broad range of target proteins. Components of the nuclear pore complex are major OGT targets, as OGT depletion by RNA interference (RNAi) results in the loss of GlcNAc modification at the nuclear envelope. To gain insight into the mechanism ...[more]

PMID: 15361863

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