Benjamin Albert

This study identifies Drs1 as a key RNA helicase that facilitates the incorporation of 25S rRNA domain III during early pre-60S ribosome maturation by interacting with Erb1 and remodeling pre-rRNA.

The paper identifies Sni445 as a novel factor that recruits snR4 and snR45 snoRNPs to 90S pre-ribosomes, enabling Kre33-mediated acetylation of 18S rRNA.

This study identifies Stm1's role in promoting ribosome biogenesis by regulating Ifh1 activity, revealing a link between ribosome biogenesis and dormancy.

This study characterizes the subcellular localization and nuclear import mechanisms of yeast RNA exosome subunits, revealing their nucleolar distribution and interactions with importins and cofactors.

This study identifies a macromolecular assembly involving snR190 and the Npa1 complex that is essential for 60S ribosomal subunit maturation in yeast.

The paper shows that Not1 and Not4 oppositely regulate mRNA solubility, affecting co-translational dynamics in yeast.

The paper addresses concerns about ChEC-seq's ability to distinguish signal from noise by demonstrating normalization methods and validating its reliability through functional assays.

This study identifies two complementary mechanisms for regulating ribosomal protein gene transcription in yeast under stress, involving Ifh1 and Sfp1, and reveals an unexpected role for Hmo1 in protein homeostasis.

The paper shows that the Tof1-Csm3 complex recruits topoisomerase I to the replisome to promote fork pausing at replication fork barriers, independent of Rrm3 helicase.

The paper shows that ribosome assembly stress triggers a pathway that balances Hsf1 and Ifh1 activity to prevent proteotoxic stress in yeast.

This study identifies Sfp1 as a master regulator of cell growth and division in yeast by coordinating gene expression through two distinct promoter binding modes.

The paper shows that RSC remodeler and pioneer factors work independently to position the +1 nucleosome at yeast promoters, facilitating transcription initiation through DNA sequence-directed action.