2010
DOI: 10.1002/bies.200900122
|View full text |Cite
|
Sign up to set email alerts
|

Eukaryotic cold shock domain proteins: highly versatile regulators of gene expression

Abstract: Cold shock domain (CSD)-containing proteins have been found in all three domains of life and function in a variety of processes that are related, for the most part, to post-transcriptional gene regulation. The CSD is an ancient beta-barrel fold that serves to bind nucleic acids. The CSD is structurally and functionally similar to the S1 domain, a fold with otherwise unrelated primary sequence. The flexibility of the CSD/S1 domain for RNA recognition confers an enormous functional versatility to the proteins th… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

2
114
0

Year Published

2011
2011
2016
2016

Publication Types

Select...
8
1

Relationship

2
7

Authors

Journals

citations
Cited by 145 publications
(119 citation statements)
references
References 84 publications
2
114
0
Order By: Relevance
“…Importantly, most (68%) of all the Lingulodinium DNA-binding domains fall into the class of cold-shock domains. However, because these domains also bind mRNA, and are better known for their role in posttranscriptional regulation in eukaryotes (17), we conclude that Lingulodinium shows a marked underrepresentation in the types of proteins and protein domains involved in regulating transcription.…”
Section: Resultsmentioning
confidence: 82%
See 1 more Smart Citation
“…Importantly, most (68%) of all the Lingulodinium DNA-binding domains fall into the class of cold-shock domains. However, because these domains also bind mRNA, and are better known for their role in posttranscriptional regulation in eukaryotes (17), we conclude that Lingulodinium shows a marked underrepresentation in the types of proteins and protein domains involved in regulating transcription.…”
Section: Resultsmentioning
confidence: 82%
“…Little is known about the regulation of gene expression in dinoflagellates, but this observation suggests that transcriptional control may not be used as extensively as in other organisms. Interestingly, the most abundant DNA-binding domain, the cold-shock domain, is also associated with posttranscriptional regulation in eukaryotes (17) and thus may not function as a DNA-binding protein at all in Lingulodinium. The idea that dinoflagellates favor regulation of gene expression at a posttranscriptional level agrees with studies on circadian regulation of protein synthesis showing extensive translation control (24,25).…”
Section: Discussionmentioning
confidence: 99%
“…64 This technique identifies phages producing a single polypeptide, and it could not have been used for NF-Y, as all three of its subunits are required for DNA binding. YB-1 was shown to be a protein with a known nucleic acid-binding domain, termed CSD (cold-shock domain), which is highly conserved in eukaryotes and prokaryotes ( Figure 1 and Mihailovich et al 65 ). Intriguingly, two cloning manuscripts published in the same period were at odds with the interpretation that YB-1 was a classic sequence-specific TF: (i) YB-1 was identified in screenings of expression libraries with a completely unrelated oligo, the W box, also from the DRa promoter, but sharing no sequence similarity to Y/CCAAT; 66 these authors first provided evidence that YB-1 binds well to single-stranded (ssDNA) and, surprisingly, to abasic DNA.…”
Section: Y and Ccaat: Two Names One Entitymentioning
confidence: 99%
“…An example of coordinated regulation is provided by the protein Upstream of N-ras (UNR), a conserved RBP involved in the regulation of mRNA stability and translation (Mihailovich et al 2010). In Drosophila, UNR contributes to opposite, sex-specific outcomes in X-chromosome dosage compensation via differential binding to RNA.…”
Section: Introductionmentioning
confidence: 99%