Cold Spring Harbor Symposia on Quantitative Biology

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ISSN / EISSN : 0091-7451 / 1943-4456
Published by: Cold Spring Harbor Laboratory (10.1101)
Total articles ≅ 5,628
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Erratum
Deirdre C. Tatomer,
Cold Spring Harbor Symposia on Quantitative Biology; https://doi.org/10.1101/sqb.2019.84.039784

Abstract:
Detailed reviews describing work presented at the annual Cold Spring Harbor Symposia on Quantitative Biology
Cold Spring Harbor Symposia on Quantitative Biology, Volume 84, pp 259-261; https://doi.org/10.1101/sqb.2019.84.039313

Abstract:
Detailed reviews describing work presented at the annual Cold Spring Harbor Symposia on Quantitative Biology
Cold Spring Harbor Symposia on Quantitative Biology, Volume 84, pp 262-263; https://doi.org/10.1101/sqb.2019.84.039032

Abstract:
Detailed reviews describing work presented at the annual Cold Spring Harbor Symposia on Quantitative Biology
Cold Spring Harbor Symposia on Quantitative Biology, Volume 84, pp 264-265; https://doi.org/10.1101/sqb.2019.84.039024

Abstract:
Detailed reviews describing work presented at the annual Cold Spring Harbor Symposia on Quantitative Biology
Cold Spring Harbor Symposia on Quantitative Biology, Volume 84, pp 274-275; https://doi.org/10.1101/sqb.2019.84.039354

Abstract:
Detailed reviews describing work presented at the annual Cold Spring Harbor Symposia on Quantitative Biology
Cold Spring Harbor Symposia on Quantitative Biology, Volume 84, pp 253-255; https://doi.org/10.1101/sqb.2019.84.039008

Abstract:
Detailed reviews describing work presented at the annual Cold Spring Harbor Symposia on Quantitative Biology
Cold Spring Harbor Symposia on Quantitative Biology, Volume 84, pp 256-258; https://doi.org/10.1101/sqb.2019.84.038992

Abstract:
Detailed reviews describing work presented at the annual Cold Spring Harbor Symposia on Quantitative Biology
Cold Spring Harbor Symposia on Quantitative Biology, Volume 84, pp 268-270; https://doi.org/10.1101/sqb.2019.84.039420

Abstract:
Detailed reviews describing work presented at the annual Cold Spring Harbor Symposia on Quantitative Biology
Xavier Rambout, Hana Cho,
Cold Spring Harbor Symposia on Quantitative Biology, Volume 84, pp 47-54; https://doi.org/10.1101/sqb.2019.84.040212

Abstract:
Mammalian cells have many quality-control mechanisms that regulate protein-coding gene expression to ensure proper transcript synthesis, processing, and translation. Should a step in transcript metabolism fail to fulfill requisite spatial, temporal, or structural criteria, including the proper acquisition of RNA-binding proteins, then that step will halt, fail to proceed to the next step, and ultimately result in transcript degradation. Quality-control mechanisms constitute a continuum of processes that initiate in the nucleus and extend to the cytoplasm. Here, we present published and unpublished data for protein-coding genes whose expression is activated by the transcriptional coactivator PGC-1α. We show that PGC-1α movement from chromatin, to which it is recruited by DNA-binding proteins, to CBP80 at the 5′ cap of nascent transcripts begins a series of co- and posttranscriptional quality- and quantity-control steps that, in total, ensure proper gene expression.
Terence T.L. Tang,
Cold Spring Harbor Symposia on Quantitative Biology, Volume 84, pp 21-30; https://doi.org/10.1101/sqb.2019.84.039818

Abstract:
The polyadenosine (poly(A)) tail, which is found on the 3′ end of almost all eukaryotic messenger RNAs (mRNAs), plays an important role in the posttranscriptional regulation of gene expression. Shortening of the poly(A) tail, a process known as deadenylation, is thought to be the first and rate-limiting step of mRNA turnover. Deadenylation is performed by the Pan2–Pan3 and Ccr4–Not complexes that contain highly conserved exonuclease enzymes Pan2, and Ccr4 and Caf1, respectively. These complexes have been extensively studied, but the mechanisms of how the deadenylase enzymes recognize the poly(A) tail were poorly understood until recently. Here, we summarize recent work from our laboratory demonstrating that the highly conserved Pan2 exonuclease recognizes the poly(A) tail, not through adenine-specific functional groups, but through the conformation of poly(A) RNA. Our biochemical, biophysical, and structural investigations suggest that poly(A) forms an intrinsic base-stacked, single-stranded helical conformation that is recognized by Pan2, and that disruption of this structure inhibits both Pan2 and Caf1. This intrinsic structure has been shown to be important in poly(A) recognition in other biological processes, further underlining the importance of the unique conformation of poly(A).
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