High impact information on MAF1

• Maf1 is an essential mediator of diverse signals that repress RNA polymerase III transcription [1].
• Signaling pathways activated in response to rapamycin-induced nutrient limitation, DNA damage, and secretory pathway defects all require Maf1 in order to affect pol III transcriptional repression [1].
• MFP1 associated factor 1 (MAF1) is a small, soluble, serine/threonine-rich protein that is ubiquitously expressed and has no similarity to known proteins [2].
• These data suggest that MFP1 and MAF1 are in vivo interaction partners and that both proteins are components of a nuclear substructure, previously undescribed in plants, that connects the nuclear envelope and the internal nuclear matrix [2].
• Finally, we report a previously undescribed phenotype for Maf1 in tRNA gene-mediated silencing of nearby RNA pol II transcription [3].

Biological context of MAF1

• In particular, mutations that prevent phosphorylation at PKA consensus sites promote nuclear accumulation of Maf1 without inducing repression [3].
• These results indicate that negative regulation of Maf1 by PKA is achieved by inhibiting its nuclear import and suggest that a PKA-independent activation step is required for nuclear Maf1 to function in the repression of pol III transcription [3].
• Maf1 is required for repression of pol III transcription in response to several signal transduction pathways and is broadly conserved in eukaryotes [4].

Associations of MAF1 with chemical compounds

• In this study, sucrose gradient analysis demonstrated that MRG15 was present in two distinct nuclear protein complexes, MAF1 (MRG15-associated factor 1) and MAF2 [5].

Other interactions of MAF1

• Maf1 is a putative repressor of RNA polymerase (pol) III transcription that is conserved from yeast to humans [1].
• Maf1 targets an Elk-1-binding site in the TBP promoter, and its occupancy of this region is reciprocal with that of Elk-1 [6].

References