BAIT

DHH1

DExD/H-box ATP-dependent RNA helicase DHH1, L000000504, YDL160C
Cytoplasmic DExD/H-box helicase, stimulates mRNA decapping; coordinates distinct steps in mRNA function and decay, interacts with both the decapping and deadenylase complexes, role in translational repression, mRNA decay, and processing body dynamics; may have a role in mRNA export; C-terminus of Dhh1p interacts with Ngr1p and promotes POR1, but not EDC1 mRNA decay; forms cytoplasmic foci upon DNA replication stress
Saccharomyces cerevisiae (S288c)
PREY

MOT2

NOT4, SIG1, CCR4-NOT core ubiquitin-protein ligase subunit MOT2, L000001887, L000001137, YER068W
Ubiquitin-protein ligase subunit of the CCR4-NOT complex; with Ubc4p, ubiquitinates nascent polypeptide-associated complex subunits and histone demethyase Jhd2p; CCR4-NOT has roles in transcription regulation, mRNA degradation, and post-transcriptional modifications; regulates levels of DNA Polymerase-{alpha} to promote efficient and accurate DNA replication
Saccharomyces cerevisiae (S288c)

Affinity Capture-RNA

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and associated RNA species identified by Northern blot, RT-PCR, affinity labeling, sequencing, or microarray analysis.

Publication

A novel translational control mechanism involving RNA structures within coding sequences.

Jungfleisch J, Nedialkova DD, Dotu I, Sloan KE, Martinez-Bosch N, Bruening L, Raineri E, Navarro P, Bohnsack MT, Leidel SA, Diez J

The impact of RNA structures in coding sequences (CDS) within mRNAs is poorly understood. Here, we identify a novel and highly conserved mechanism of translational control involving RNA structures within coding sequences and the DEAD-box helicase Dhh1. Using yeast genetics and genome-wide ribosome profiling analyses, we show that this mechanism, initially derived from studies of the Brome Mosaic virus RNA ... [more]

Genome Res. Dec. 01, 2016; 27(1);95-106 [Pubmed: 27821408]

Throughput

  • High Throughput

Additional Notes

  • CRAC

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
MOT2 DHH1
Affinity Capture-MS
Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

Low-BioGRID
-
DHH1 MOT2
Affinity Capture-RNA
Affinity Capture-RNA

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and associated RNA species identified by Northern blot, RT-PCR, affinity labeling, sequencing, or microarray analysis.

High-BioGRID
-
DHH1 MOT2
Affinity Capture-RNA
Affinity Capture-RNA

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and associated RNA species identified by Northern blot, RT-PCR, affinity labeling, sequencing, or microarray analysis.

High-BioGRID
812059
DHH1 MOT2
PCA
PCA

A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.

High-BioGRID
-
DHH1 MOT2
Synthetic Lethality
Synthetic Lethality

A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition.

Low-BioGRID
157961

Curated By

  • BioGRID