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Multiple polyadenylation signals and 3' untranslated sequences are conserved between chicken and human cellular myosin II transcripts.

ABSTRACT: We have isolated a chicken cellular myosin II heavy chain isoform cDNA clone that overlaps the published sequence for MHC-A (Shohet et al., 1989, Proc Natl Acad Sci 86, 7726-7730) and contains three canonical AAUAAA-polyadenylation signals in an additional 374 nucleotides at its 3' end. S1 nuclease protection analysis and PCR-amplification of MHC-A cDNA 3' ends have confirmed that all three of the signals are used in vivo. Differential usage of these signals without differential splicing in this region yields three messages that differ at their 3' ends but appear to encode the same protein. Comparison of the new chicken sequence with the homologous human MHC-A cDNA sequence (Saez et al., 1990, Proc Natl Acad Sci 87, 1164-1168) has revealed a number of similarities at this end of their long 3' untranslated regions (3'-UTRs). The three chicken polyadenylation signals reported here are positioned similarly to three signals evident in the human sequence. This region also contains distinct stretches of identity that are interspersed with regions of little homology. Within these regions of identity are a number of conserved sequence motifs, some of which have been demonstrated to be involved in mRNA metabolism in other systems. The pattern of mRNA sequence conservation demonstrated here suggests that the mechanisms for regulating MHC-A mRNA metabolism have been conserved between chickens and humans.

SUBMITTER: Volosky JM

PROVIDER: S-EPMC5952193 | biostudies-literature | 1991

REPOSITORIES: biostudies-literature

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Multiple polyadenylation signals and 3' untranslated sequences are conserved between chicken and human cellular myosin II transcripts.

Volosky J M JM Keller T C TC

Gene expression 19910101 3

We have isolated a chicken cellular myosin II heavy chain isoform cDNA clone that overlaps the published sequence for MHC-A (Shohet et al., 1989, Proc Natl Acad Sci 86, 7726-7730) and contains three canonical AAUAAA-polyadenylation signals in an additional 374 nucleotides at its 3' end. S1 nuclease protection analysis and PCR-amplification of MHC-A cDNA 3' ends have confirmed that all three of the signals are used in vivo. Differential usage of these signals without differential splicing in this ...[more]

PMID: 1687916

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Project description:Recent biochemical studies of p190, a calmodulin (CM)-binding protein purified from vertebrate brain, have demonstrated that this protein, purified as a complex with bound CM, shares a number of properties with myosins (Espindola, F. S., E. M. Espreafico, M. V. Coelho, A. R. Martins, F. R. C. Costa, M. S. Mooseker, and R. E. Larson. 1992. J. Cell Biol. 118:359-368). To determine whether or not p190 was a member of the myosin family of proteins, a set of overlapping cDNAs encoding the full-length protein sequence of chicken brain p190 was isolated and sequenced. Verification that the deduced primary structure was that of p190 was demonstrated through microsequence analysis of a cyanogen bromide peptide generated from chick brain p190. The deduced primary structure of chicken brain p190 revealed that this 1,830-amino acid (aa) 212,509-D) protein is a member of a novel structural class of unconventional myosins that includes the gene products encoded by the dilute locus of mouse and the MYO2 gene of Saccharomyces cerevisiae. We have named the p190-CM complex "myosin-V" based on the results of a detailed sequence comparison of the head domains of 29 myosin heavy chains (hc), which has revealed that this myosin, based on head structure, is the fifth of six distinct structural classes of myosin to be described thus far. Like the presumed products of the mouse dilute and yeast MYO2 genes, the head domain of chicken myosin-V hc (aa 1-764) is linked to a "neck" domain (aa 765-909) consisting of six tandem repeats of an approximately 23-aa "IQ-motif." All known myosins contain at least one such motif at their head-tail junctions; these IQ-motifs may function as calmodulin or light chain binding sites. The tail domain of chicken myosin-V consists of an initial 511 aa predicted to form several segments of coiled-coil alpha helix followed by a terminal 410-aa globular domain (aa, 1,421-1,830). Interestingly, a portion of the tail domain (aa, 1,094-1,830) shares 58% amino acid sequence identity with a 723-aa protein from mouse brain reported to be a glutamic acid decarboxylase. The neck region of chicken myosin-V, which contains the IQ-motifs, was demonstrated to contain the binding sites for CM by analyzing CM binding to bacterially expressed fusion proteins containing the head, neck, and tail domains. Immunolocalization of myosin-V in brain and in cultured cells revealed an unusual distribution for this myosin in both neurons and nonneuronal cells.(ABSTRACT TRUNCATED AT 400 WORDS)

Dataset Information

Multiple polyadenylation signals and 3' untranslated sequences are conserved between chicken and human cellular myosin II transcripts.

Publications

Multiple polyadenylation signals and 3' untranslated sequences are conserved between chicken and human cellular myosin II transcripts.

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