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• W1994642993 abstract "The C-terminal globular head of the lollipop-shaped σ1 protein of reovirus is responsible for interaction with the host cell receptor. Like the N-terminal fibrous tail, it has its own trimerization domain. Whereas N-terminal trimerization (formation of a triple α-helical coiled coil) occurs at the level of polysomes (i.e. cotranslationally) and is ATP-independent, C-terminal trimerization is a posttranslational event that requires ATP. Coprecipitation experiments using anti-Hsp70 antibodies and truncated σ1 proteins synthesized in vitro revealed that only regions downstream of the N-terminal α-helical coiled coil were associated with Hsp70. Hsp70 was also found to be associated with nascent σ1 chains on polysomes as well as with immature postribosomal σ1 trimers (hydra-like intermediates with assembled N termini and unassembled C termini). These latter structures were true intermediates in the σ1 biogenetic pathway since they could be chased into mature σ1 trimers with the release of Hsp70. Thus, unlike N-terminal trimerization, C-terminal trimerization is Hsp70- and ATP-dependent. The involvement of two mechanistically distinct oligomerization events for the same molecule, one cotranslational and one posttranslational, may represent a common approach to the generation of oligomeric proteins in the cytosol. The C-terminal globular head of the lollipop-shaped σ1 protein of reovirus is responsible for interaction with the host cell receptor. Like the N-terminal fibrous tail, it has its own trimerization domain. Whereas N-terminal trimerization (formation of a triple α-helical coiled coil) occurs at the level of polysomes (i.e. cotranslationally) and is ATP-independent, C-terminal trimerization is a posttranslational event that requires ATP. Coprecipitation experiments using anti-Hsp70 antibodies and truncated σ1 proteins synthesized in vitro revealed that only regions downstream of the N-terminal α-helical coiled coil were associated with Hsp70. Hsp70 was also found to be associated with nascent σ1 chains on polysomes as well as with immature postribosomal σ1 trimers (hydra-like intermediates with assembled N termini and unassembled C termini). These latter structures were true intermediates in the σ1 biogenetic pathway since they could be chased into mature σ1 trimers with the release of Hsp70. Thus, unlike N-terminal trimerization, C-terminal trimerization is Hsp70- and ATP-dependent. The involvement of two mechanistically distinct oligomerization events for the same molecule, one cotranslational and one posttranslational, may represent a common approach to the generation of oligomeric proteins in the cytosol." @default.
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• W1994642993 date "1996-04-01" @default.
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• W1994642993 title "C-terminal Trimerization, but Not N-terminal Trimerization, of the Reovirus Cell Attachment Protein Is a Posttranslational and Hsp70/ATP-dependent Process" @default.
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• W1994642993 doi "https://doi.org/10.1074/jbc.271.14.8466" @default.
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