Recombinant Saccharomyces cerevisiae Uncharacterized endoplasmic reticulum membrane protein YMR122W-A (YMR122W-A)
Description
Introduction to Recombinant Saccharomyces cerevisiae Uncharacterized Endoplasmic Reticulum Membrane Protein YMR122W-A
YMR122W-A is a poorly characterized transmembrane protein localized to the endoplasmic reticulum (ER) and cytoplasm in Saccharomyces cerevisiae (baker’s yeast) . Originally identified through proteome-wide profiling, it exhibits selective expression under specific growth conditions, such as raffinose, and is implicated in ER-associated processes, including protein glycosylation and translation regulation . Recombinant versions of this protein are commercially available for research purposes, often tagged with His for purification and expressed in Escherichia coli .
Amino Acid Composition and Localization
YMR122W-A contains 84 amino acids (AA) with a predicted transmembrane domain flanked by cytoplasmic and non-cytoplasmic regions . Its GFP-fusion protein localizes to both the ER and cytoplasm, suggesting dynamic subcellular distribution .
Hypothesized Roles in ER Processes
YMR122W-A may interact with ER-resident glycosyltransferases (e.g., PMT1, CBR1) to regulate protein glycosylation, particularly under stress or nutrient shifts . Its paralogue, MNN4 (a mannosyltransferase), is linked to cell wall thickening in stationary phase, suggesting a conserved role in glycosylation .
Translation Regulation
Mutational studies reveal that synonymous codon changes in YMR122W-A alter ribosome density at the A-site, indicating potential modulation of translation speed . For example, substituting proline (slow-translating) with glutamic acid in the P-site accelerates translation, while other amino acid substitutions (e.g., glutamine to proline) slow it .
Genetic Interactions
A positive genetic interaction with CLP1 (a mitochondrial ATP-dependent protease) suggests functional cooperation in cellular stress responses or organelle maintenance .
Ribosome Profiling Studies
YMR122W-A serves as a model for studying how P-site amino acids influence translation efficiency. Mutations in codon pairs (e.g., (Q,D) → (P,D)) reduce ribosome density at the A-site, supporting a role in translation elongation control .
RNA Termination and Sen1 Pathway
In sen1 mutants, read-through transcripts of the YMR122W-A ORF are observed, implicating this protein in RNA termination mechanisms . Sen1, a helicase involved in transcriptional termination, may regulate YMR122W-A mRNA stability .
Product Specs
Note: While we prioritize shipping the format currently in stock, please specify your preferred format in order notes for customized fulfillment.
Note: All proteins are shipped with standard blue ice packs. Dry ice shipping requires prior arrangement and incurs additional charges.
The tag type is determined during the production process. If you require a specific tag, please inform us, and we will prioritize its development.
Target Background
KEGG: sce:YMR122W-A
STRING: 4932.YMR122W-A
