Use of the ND evidence code for Gene Ontology (GO) terms
Annotation inferences using phylogenetic trees
Yeast hEST1A/B (SMG5/6)-like proteins contribute to environment-sensing adaptive gene expression responses.
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Esl1 (Yil151c) and its paralog Esl2 (Ykr096w) are structural orthologs of metazoan hEST1A/B (SMG5/6), sharing a 14-3-3-like Est-one-homology domain and a C-terminal PIN endonuclease domain with the four conserved catalytic acidic residues.
"this similarity encompassed the region corresponding to the 14-3-3–like Est-one-homology domain (45–51% similarity; Figure 1, A and B) and the C-terminal PIN endonuclease domain (49–53% similarity; Figure 1, A and C) with complete conservation of four critical D/E residues required for nuclease activity of the PIN-domain proteins"
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Single/double mutants showed no defect in the tested NMD-substrate and telomere-maintenance assays; these phenotype measurements did not test DNA/RNA binding or complex incorporation.
"unlike their metazoan orthologs, Esl1 and Esl2 were not involved in nonsense-mediated mRNA decay or telomere maintenance pathways"
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Loss of Esl1 and Esl2 deregulates ~50 transcripts, most expressed inversely to the appropriate metabolic response to environmental nutrient supply.
"absence of Esl1 and Esl2 led to more than two-fold deregulation of ∼50 transcripts, most of which were expressed inversely to the appropriate metabolic response to environmental nutrient supply"
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esl1 esl2 double mutants are synthetic sick with rim8 and dfg16, components of the Rim101 pH-response environmental-sensing pathway.
"esl1Δ esl2Δ double mutants were synthetic sick with null mutations for Rim8 and Dfg16, which form the environmental-sensing complex of the Rim101 pH response gene expression pathway"
Global analysis of protein expression in yeast.
A multidimensional chromatography technology for in-depth phosphoproteome analysis.
ESL1: inspected PAINT ancestry
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Actual accession-mapped ancestry was checked, independently of subfamily labels and donor counts.
"All four inherited annotations originate at PTN000403280 and are still positive on target leaf PTN007651903."
UniProt P40456 ESL1 record
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Esl1 protein is expressed at a low level (~504 molecules/cell) in log-phase SD medium.
"Present with 504 molecules/cell in log phase SD medium."
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Esl1 is phosphorylated at Ser-170 and Ser-190 (large-scale phosphoproteomics).
"PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND SER-190"
Falcon literature report for yeast ESL1
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The report explicitly lacked the dedicated Lai 2013 paper and therefore inferred functions from other EST/SMG proteins.
"which could not be fully accessed during this literature search."
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Its suggestion that Esl1 alone is the yeast PIN-containing family member overlooks the directly characterized Esl2 paralog.
"ESL1 is notable as the only yeast family member annotated as possessing a PIN domain, making it structurally distinct from its yeast paralogs."
OpenScientist focused assessment of ESL1 telomerase association and nucleic-acid binding
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The report recommends removing the three inherited telomerase MF/CC terms while acknowledging that direct target binding assays are absent and that the primary full texts were not read. It supplies STRING channel and global sequence-identity tables, but no executable analysis or aligned sequences. These are useful leads and scope limits, not a demonstrated ancestral loss.
"full text of the two primary papers was not read"
Functional analysis of the single Est1/Ebs1 homologue in Kluyveromyces lactis reveals roles in both telomere maintenance and rapamycin resistance.
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Purified Kluyveromyces lactis Est1 N-terminal domain contacts Ter1 RNA in a UV-crosslinking assay (Fig.4), although EMSA did not recover a complex. This is a positive paralog/comparator assay, not a test of Saccharomyces Esl1 or evidence that only the Est1/Ebs1 branch can bind telomerase RNA.
"we were able to demonstrate a direct physical interaction between Est1"