Link to this page
Human Interaction Network Ontology
| Preferred Name | Activation of the pre-replicative complex | |
| Synonyms |
|
|
| Definitions |
In S. cerevisiae, two ORC subunits, Orc1 and Orc5, both bind ATP, and Orc1 in addition has ATPase activity. Both ATP binding and ATP hydrolysis appear to be essential functions in vivo. ATP binding by Orc1 is unaffected by the association of ORC with origin DNA (ARS) sequences, but ATP hydrolysis is ARS-dependent, being suppressed by associated double-stranded DNA and stimulated by associated single-stranded DNA. These data are consistent with the hypothesis that ORC functions as an ATPase switch, hydrolyzing bound ATP and changing state as DNA unwinds at the origin immediately before replication. It is attractive to speculate that ORC likewise functions as a switch as human pre-replicative complexes are activated, but human Orc proteins are not well enough characterized to allow the model to be critically tested. mRNAs encoding human orthologs of all six Orc proteins have been cloned, and ATP-binding amino acid sequence motifs have been identified in Orc1, Orc4, and Orc5. Interactions among proteins expressed from the cloned genes have been characterized, but the ATP-binding and hydrolyzing properties of these proteins and complexes of them have not been determined. |
|
| ID |
http://purl.obolibrary.org/obo/HINO_0015245 |
|
| comment |
In S. cerevisiae, two ORC subunits, Orc1 and Orc5, both bind ATP, and Orc1 in addition has ATPase activity. Both ATP binding and ATP hydrolysis appear to be essential functions in vivo. ATP binding by Orc1 is unaffected by the association of ORC with origin DNA (ARS) sequences, but ATP hydrolysis is ARS-dependent, being suppressed by associated double-stranded DNA and stimulated by associated single-stranded DNA. These data are consistent with the hypothesis that ORC functions as an ATPase switch, hydrolyzing bound ATP and changing state as DNA unwinds at the origin immediately before replication. It is attractive to speculate that ORC likewise functions as a switch as human pre-replicative complexes are activated, but human Orc proteins are not well enough characterized to allow the model to be critically tested. mRNAs encoding human orthologs of all six Orc proteins have been cloned, and ATP-binding amino acid sequence motifs have been identified in Orc1, Orc4, and Orc5. Interactions among proteins expressed from the cloned genes have been characterized, but the ATP-binding and hydrolyzing properties of these proteins and complexes of them have not been determined.
|
|
| definition source |
Pubmed11395502 Pubmed7502077 Pubmed10402192 Pubmed12169736 Reactome, http://www.reactome.org Pubmed10801458 Pubmed11323433 Pubmed9765232 Pubmed9829972 Pubmed9038340 Pubmed9353276 Pubmed10970868 Pubmed11779870 Pubmed11459976
|
|
| label |
Activation of the pre-replicative complex
|
|
| located_in | ||
| prefixIRI |
HINO:0015245
|
|
| prefLabel |
Activation of the pre-replicative complex
|
|
| seeAlso |
ReactomeREACT_1095 Reactome Database ID Release 4368962
|
|
| subClassOf | ||
| has_part |
http://purl.obolibrary.org/obo/HINO_0014870 http://purl.obolibrary.org/obo/HINO_0014871 http://purl.obolibrary.org/obo/HINO_0014872 http://purl.obolibrary.org/obo/HINO_0014867 http://purl.obolibrary.org/obo/HINO_0014868 http://purl.obolibrary.org/obo/HINO_0014866 |
| Delete | Subject | Author | Type | Created |
|---|---|---|---|---|
| No notes to display |