Unknown

Dataset Information

0

Molecular architecture of the human pre-mRNA 3' processing complex.


ABSTRACT: Pre-mRNA 3' end formation is an essential step in eukaryotic gene expression. Over half of human genes produce alternatively polyadenylated mRNAs, suggesting that regulated polyadenylation is an important mechanism for posttranscriptional gene control. Although a number of mammalian mRNA 3' processing factors have been identified, the full protein composition of the 3' processing machinery has not been determined, and its structure is unknown. Here we report the purification and subsequent proteomic and structural characterization of human mRNA 3' processing complexes. Remarkably, the purified 3' processing complex contains approximately 85 proteins, including known and new core 3' processing factors and over 50 proteins that may mediate crosstalk with other processes. Electron microscopic analyses show that the core 3' processing complex has a distinct "kidney" shape and is approximately 250 A in length. Together, our data has revealed the complexity and molecular architecture of the pre-mRNA 3' processing complex.

SUBMITTER: Shi Y 

PROVIDER: S-EPMC2946185 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

Molecular architecture of the human pre-mRNA 3' processing complex.

Shi Yongsheng Y   Di Giammartino Dafne Campigli DC   Taylor Derek D   Sarkeshik Ali A   Rice William J WJ   Yates John R JR   Frank Joachim J   Manley James L JL  

Molecular cell 20090201 3


Pre-mRNA 3' end formation is an essential step in eukaryotic gene expression. Over half of human genes produce alternatively polyadenylated mRNAs, suggesting that regulated polyadenylation is an important mechanism for posttranscriptional gene control. Although a number of mammalian mRNA 3' processing factors have been identified, the full protein composition of the 3' processing machinery has not been determined, and its structure is unknown. Here we report the purification and subsequent prote  ...[more]

Similar Datasets

| S-EPMC3759880 | biostudies-literature
| S-EPMC2874999 | biostudies-literature
| S-EPMC1905900 | biostudies-literature
| S-EPMC2169417 | biostudies-literature
| S-EPMC7036032 | biostudies-literature
| S-EPMC2863591 | biostudies-literature
| S-EPMC3482686 | biostudies-literature
| S-EPMC8668186 | biostudies-literature
| S-EPMC7008720 | biostudies-literature
| S-EPMC5788269 | biostudies-literature