Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction.
Sequence database searches, using iterative-profile and Hidden-Markov-model approaches, were used to detect hitherto-undetected homologues of proteins that regulate the endoplasmic reticulum (ER)-associated degradation pathway. The translocon-associated subunit Sec63p (Sec=secretory) was shown to co...
| Main Author: | |
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| Format: | Journal article |
| Language: | English |
| Published: |
2000
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| _version_ | 1797071274707517440 |
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| author | Ponting, C |
| author_facet | Ponting, C |
| author_sort | Ponting, C |
| collection | OXFORD |
| description | Sequence database searches, using iterative-profile and Hidden-Markov-model approaches, were used to detect hitherto-undetected homologues of proteins that regulate the endoplasmic reticulum (ER)-associated degradation pathway. The translocon-associated subunit Sec63p (Sec=secretory) was shown to contain a domain of unknown function found twice in several Brr2p-like RNA helicases (Brr2=bad response to refrigeration 2). Additionally, Cue1p (Cue=coupling of ubiquitin conjugation to ER degradation), a yeast protein that recruits the ubiquitin-conjugating (UBC) enzyme Ubc7p to an ER-associated complex, was found to be one of a large family of putative scaffolding-domain-containing proteins that include the autocrine motility factor receptor and fungal Vps9p (Vps=vacuolar protein sorting). Two other yeast translocon-associated molecules, Sec72p and Hrd3p (Hrd=3-hydroxy-3-methylglutaryl-CoA reductase degradation), were shown to contain multiple tetratricopeptide-repeat-like sequences. From this observation it is suggested that Sec72p associates with a heat-shock protein, Hsp70, in a manner analogous to that known for Hop (Hsp70/Hsp90 organizing protein). Finally, the luminal portion of Ire1p (Ire=high inositol-requiring), thought to convey the sensing function of this transmembrane kinase and endoribonuclease, was shown to contain repeats similar to those in beta-propeller proteins. This finding hints at the mechanism by which Ire1p may sense extended unfolded proteins at the expense of compact folded molecules. |
| first_indexed | 2024-03-06T22:50:56Z |
| format | Journal article |
| id | oxford-uuid:5ebfbcec-52b8-4103-a72a-fdc3cd1178e6 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:50:56Z |
| publishDate | 2000 |
| record_format | dspace |
| spelling | oxford-uuid:5ebfbcec-52b8-4103-a72a-fdc3cd1178e62022-03-26T17:42:38ZProteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:5ebfbcec-52b8-4103-a72a-fdc3cd1178e6EnglishSymplectic Elements at Oxford2000Ponting, CSequence database searches, using iterative-profile and Hidden-Markov-model approaches, were used to detect hitherto-undetected homologues of proteins that regulate the endoplasmic reticulum (ER)-associated degradation pathway. The translocon-associated subunit Sec63p (Sec=secretory) was shown to contain a domain of unknown function found twice in several Brr2p-like RNA helicases (Brr2=bad response to refrigeration 2). Additionally, Cue1p (Cue=coupling of ubiquitin conjugation to ER degradation), a yeast protein that recruits the ubiquitin-conjugating (UBC) enzyme Ubc7p to an ER-associated complex, was found to be one of a large family of putative scaffolding-domain-containing proteins that include the autocrine motility factor receptor and fungal Vps9p (Vps=vacuolar protein sorting). Two other yeast translocon-associated molecules, Sec72p and Hrd3p (Hrd=3-hydroxy-3-methylglutaryl-CoA reductase degradation), were shown to contain multiple tetratricopeptide-repeat-like sequences. From this observation it is suggested that Sec72p associates with a heat-shock protein, Hsp70, in a manner analogous to that known for Hop (Hsp70/Hsp90 organizing protein). Finally, the luminal portion of Ire1p (Ire=high inositol-requiring), thought to convey the sensing function of this transmembrane kinase and endoribonuclease, was shown to contain repeats similar to those in beta-propeller proteins. This finding hints at the mechanism by which Ire1p may sense extended unfolded proteins at the expense of compact folded molecules. |
| spellingShingle | Ponting, C Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction. |
| title | Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction. |
| title_full | Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction. |
| title_fullStr | Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction. |
| title_full_unstemmed | Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction. |
| title_short | Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction. |
| title_sort | proteins of the endoplasmic reticulum associated degradation pathway domain detection and function prediction |
| work_keys_str_mv | AT pontingc proteinsoftheendoplasmicreticulumassociateddegradationpathwaydomaindetectionandfunctionprediction |