PMC:2728203 / 21010-22166 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/2728203","sourcedb":"PMC","sourceid":"2728203","source_url":"https://www.ncbi.nlm.nih.gov/pmc/2728203","text":"In summary, our results show that the N-terminal domain of Nab2 binds to the C-terminal domain of Mlp1 and that the Mlp1 binding site on Nab2 does not appear to overlap with the Gfd1 binding site. The Nab2 N-terminal domain has a fold based on a five-helix bundle that is analogous to the PWI fold found in SRm160 and other nucleic acid binding proteins, although it does not retain the nucleic acid binding function seen in other PWI domains. The hydrophobic side chain of Phe73 in the Nab2 N-terminal domain is exposed on the surface of the molecule and appears to be a crucial component of the Mlp1 binding site, although, clearly, further work will be required to define the precise nature of the interface between these two molecules. Our results are consistent with a model that envisages that interaction with Mlp proteins occurs soon before mRNA is exported and that Nab2 is important either for targeting the mRNA to the Mlp proteins or for releasing the mature mRNA from the Mlp proteins to enable its transit through the NPC. Such a model would be consistent with the increased nuclear retention of mRNA seen on overexpression of Mlp1 in vivo.21","tracks":[{"project":"2_test","denotations":[{"id":"18190927-12531921-62517992","span":{"begin":1154,"end":1156},"obj":"12531921"}],"attributes":[{"subj":"18190927-12531921-62517992","pred":"source","obj":"2_test"}]}],"config":{"attribute types":[{"pred":"source","value type":"selection","values":[{"id":"2_test","color":"#ec9394","default":true}]}]}}