| + |
HBS1L | form complex 
binding
|
Pelota-HBS1L ribosome dissociation complex |
0.618 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281437 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21448132 |
No-go decay (NGD) and non-stop decay (NSD) are eukaryotic surveillance mechanisms that target mRNAs on which elongation complexes (ECs) are stalled by, for example, stable secondary structures (NGD) or due to the absence of a stop codon (NSD). Two interacting proteins Dom34(yeast)/Pelota(mammals) and Hbs1, which are paralogues of eRF1 and eRF3, are implicated in these processes. Dom34/Hbs1 were shown to promote dissociation of stalled ECs and release of intact peptidyl-tRNA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PELO | form complex
binding
|
Pelota-HBS1L ribosome dissociation complex |
0.694 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281435 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21448132 |
No-go decay (NGD) and non-stop decay (NSD) are eukaryotic surveillance mechanisms that target mRNAs on which elongation complexes (ECs) are stalled by, for example, stable secondary structures (NGD) or due to the absence of a stop codon (NSD). Two interacting proteins Dom34(yeast)/Pelota(mammals) and Hbs1, which are paralogues of eRF1 and eRF3, are implicated in these processes. Dom34/Hbs1 were shown to promote dissociation of stalled ECs and release of intact peptidyl-tRNA. Using an in vitro reconstitution approach, we investigated the activities of mammalian Pelota/Hbs1 and report that Pelota/Hbs1 also induced dissociation of ECs and release of peptidyl-tRNA, but only in the presence of ABCE1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ABCE1 | form complex
binding
|
Pelota-HBS1L ribosome dissociation complex |
0.587 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281436 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21448132 |
No-go decay (NGD) and non-stop decay (NSD) are eukaryotic surveillance mechanisms that target mRNAs on which elongation complexes (ECs) are stalled by, for example, stable secondary structures (NGD) or due to the absence of a stop codon (NSD). Two interacting proteins Dom34(yeast)/Pelota(mammals) and Hbs1, which are paralogues of eRF1 and eRF3, are implicated in these processes. Dom34/Hbs1 were shown to promote dissociation of stalled ECs and release of intact peptidyl-tRNA. Using an in vitro reconstitution approach, we investigated the activities of mammalian Pelota/Hbs1 and report that Pelota/Hbs1 also induced dissociation of ECs and release of peptidyl-tRNA, but only in the presence of ABCE1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Pelota-HBS1L ribosome dissociation complex | down-regulates quantity by destabilization 
binding
|
80S_cytosolic_ribosome |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281438 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21448132 |
No-go decay (NGD) and non-stop decay (NSD) are eukaryotic surveillance mechanisms that target mRNAs on which elongation complexes (ECs) are stalled by, for example, stable secondary structures (NGD) or due to the absence of a stop codon (NSD). Two interacting proteins Dom34(yeast)/Pelota(mammals) and Hbs1, which are paralogues of eRF1 and eRF3, are implicated in these processes. Dom34/Hbs1 were shown to promote dissociation of stalled ECs and release of intact peptidyl-tRNA. ABCE1/Pelota/Hbs1 also dissociated vacant 80S ribosomes, which stimulated 48S complex formation, suggesting that Pelota/Hbs1 have an additional role outside of NGD. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
Pelota-HBS1L ribosome dissociation complex