Dataset Information

Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum.

ABSTRACT: Eukaryotic secretory pathway cargo fold to their native structures within the confines of the endoplasmic reticulum (ER). To ensure a high degree of folding fidelity, a multitude of covalent and noncovalent constraints are imparted upon nascent proteins. These constraints come in the form of topological restrictions or membrane tethers, covalent modifications, and interactions with a series of molecular chaperones. N-linked glycosylation provides inherent benefits to proper folding and creates a platform for interactions with specific chaperones and Cys modifying enzymes. Recent insights into this timeline of protein maturation have revealed mechanisms for protein glycosylation and iterative targeting of incomplete folding intermediates, which provides nurturing interactions with molecular chaperones that assist in the efficient maturation of proteins in the eukaryotic secretory pathway.

SUBMITTER: Pearse BR

PROVIDER: S-EPMC2875293 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature

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Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum.

Pearse Bradley R BR Hebert Daniel N DN

Biochimica et biophysica acta 20091103 6

Eukaryotic secretory pathway cargo fold to their native structures within the confines of the endoplasmic reticulum (ER). To ensure a high degree of folding fidelity, a multitude of covalent and noncovalent constraints are imparted upon nascent proteins. These constraints come in the form of topological restrictions or membrane tethers, covalent modifications, and interactions with a series of molecular chaperones. N-linked glycosylation provides inherent benefits to proper folding and creates a ...[more]

PMID: 19891995

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Project description:Aim and experimental set-up: Sequencing of small RNA from total RNA fractions. The aim of this experiment was to compare profiles of miRNA expression between the following genetic backgrounds: Col-0 (wild type), era1-2 (farnesyl transferase mutant), j2-2/j3-2 + pJ3:J3 (j2/j3 double knockout expressing transgenic J3 under the control of the endogenous J3 promoter), j2-2/j3-2 + pJ3:J3C417S (j2/j3 double knockout expressing transgenic J3 mutated in the farnesylation site (C417S) under the control of the endogenous J3 promoter). Seedlings were grown under sterile conditions for 16 days. Two biological replicates of each genotype were harvested, and total RNA was prepared by Trizol extraction. Small RNA libraries were constructed using NEBNext Small RNA Library Prep Set and sequenced on an Illumina platform. Sequencing of small RNA bound to AGO1 in membrane fractions The aim of this experiment was to characterize AGO1-bound small RNAs in membrane fractions, and to answer two specific questions: Can miRNAs be identified whose association with membrane-bound AGO1 is different between the following four genotypes: Col-0 (wild type), era1-2 (farnesyl transferase mutant), j2-2/j3-2 + pJ3:J3 (j2/j3 double knockout expressing transgenic J3 under the control of the endogenous J3 promoter), j2-2/j3-2 + pJ3:J3C417S (j2/j3 double knockout expressing transgenic J3 mutated in the farnesylation site (C417S) under the control of the endogenous J3 promoter) Is the ratio between reads matching miRNA and miRNA* different between the above four genotypes? Seedlings were grown under sterile conditions for 16 days. Two biological replicates of each genotype were harvested. Microsomes were prepared from 2g of seedling tissue, solubilized by 1% deoxycholate and AGO1 was immunoprecipitated with specific antibodies (Agrisera). Immunopurified AGO1 was eluted from Protein A sepharose beads by competitive elution with antigenic AGO1 peptide. Small RNA was extracted by Trizol extraction from eluted AGO1. Small RNA libraries were constructed using NEBNext Small RNA Library Prep Set and sequenced on an Illumina platform.

Dataset Information

Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum.

Publications

Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum.

Similar Datasets

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