3′ Non-coding region sequences in eukaryotic messenger RNA

Proudfoot, Nicholas J.; Brownlee, George G.

doi:10.1038/263211a0

Cited by 3,007 publications

(1,120 citation statements)

References 23 publications

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“…The polyadenylation signal (PAS)-The PAS was the first identified sequence element proposed to play a role in 3′-end processing [37]. This AAUAAA hexamer was found in 80-90% of sequenced mRNAs.…”

Section: Sequence Elements In Mammalsmentioning

confidence: 99%

Protein factors in pre-mRNA 3′-end processing

Mandel

Bai

Tong

2007

Cell. Mol. Life Sci.

352

482

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Most eukaryotic mRNA precursors (pre-mRNAs) must undergo extensive processing, including cleavage and polyadenylation at the 3′-end. Processing at the 3′-end is controlled by sequence elements in the pre-mRNA (cis elements) as well as protein factors. Despite the seeming biochemical simplicity of the processing reactions, more than 14 proteins have been identified for the mammalian complex, and more than 20 proteins have been identified for the yeast complex. The 3′-end processing machinery also has important roles in transcription and splicing. The mammalian machinery contains several sub-complexes, including cleavage and polyadenylation specificity factor (CPSF), cleavage stimulation factor (CstF), cleavage factor I (CF I m ), and cleavage factor II (CF II m ). Additional protein factors include poly(A) polymerase (PAP), poly(A) binding protein (PABP), symplekin, and the C-terminal domain (CTD) of RNA polymerase II largest subunit. The yeast machinery includes cleavage factor IA (CF IA), cleavage factor IB (CF IB), and cleavage and polyadenylation factor (CPF).

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Section: Sequence Elements In Mammalsmentioning

confidence: 99%

Protein factors in pre-mRNA 3′-end processing

Mandel

Bai

Tong

2007

Cell. Mol. Life Sci.

352

482

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“…If transcripts initiating at these sites were to have no functional splice sites 5' of the junction between exon II and the following intron, then the processed RNAs would range in size from 1,660 to 2,450 nucleotides (not including the poly(A) tail 28 ). That this is the case is suggested by cDNA cloning, which has revealed a contiguous transcript extending upstream from exon II at least as far as position 660.…”

Section: C-myc Translocation In Manca Cellsmentioning

confidence: 99%

Activation of a translocated human c-myc gene by an enhancer in the immunoglobulin heavy-chain locus

Hayday

Gillies

Saito

et al. 1984

Nature

257

112

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“…The FPV hemagglutinin is terminated by a single UAA signal. Neither hemagglutinin gene contains the AAUAAA sequence found at a short distance preceding the poly(A) tail of all eucaryotic cellular and many viral messengers [and possibly implicated in the polyadenylation process (Proudfoot and Brownlee, 1976)]. The majority of picornaviruses (Porter et al, 1978) and one of the VSV mRNAs (McGeoch and Turnbull, 1978) also do not have this signal.…”

mentioning

confidence: 99%

Complete structure of the hemagglutinin gene from the human influenza A/Victoria/3/75 (H3N2) strain as determined from cloned DNA

Jou

Verhoeyen

Devos

et al. 1980

Cell

219

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SummaryThe complete sequence of a hemagglutinin (HA) gene of a recent human influenza A strain, A/Victoria/3/75, is 1768 nucleotides long and contains the information for 567 amino acids. It codes for a signal peptide of 16 amino acids, the HA1 chain of the mature hemagglutinin of 329 amino acids, a connecting region between HA1 and HA2 consisting of a single arginine residue and the HA2 portion of 221 amino acids. The sequence is compared with the hemagglutinin of two members of other subtypes, the human H2 strain A/Jap/305/57 and the avian Havl strain A/FPV/Rostock/34, and with one of the same H3 subtype, A/Memphis/3/72. To align the HA1 chain of different major subtypes several deletions/insertions of single amino acids must be invoked, but two more extensive differences are found at both ends, one leading to an extension of the amino terminal sequence of HA1 and the other (four residues) occurring in the region processed away between HA1 and HA2. Comparison of the HA1 of two H3 strains suggests that drift probably depends on single base mutations, some of which change antigenic determinants. The HA2 region, which apparently is not involved in the immune response, is highly conserved even between different subtypes, and single base substitutions account for all the observed diversity. A hydrophobic segment of 24 residues is present in the same position close to the carboxyl terminus of HA2 in both Victoria and FPV, and presumably functions in implantation into the lipid bilayer. The many conserved features not only in HA2 but also in HA1 suggest a rather rigid architecture for the whole hemagglutinin molecule.

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3′ Non-coding region sequences in eukaryotic messenger RNA

Cited by 3,007 publications

References 23 publications

Protein factors in pre-mRNA 3′-end processing

Protein factors in pre-mRNA 3′-end processing

Activation of a translocated human c-myc gene by an enhancer in the immunoglobulin heavy-chain locus

Complete structure of the hemagglutinin gene from the human influenza A/Victoria/3/75 (H3N2) strain as determined from cloned DNA

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