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RNA-mediated RNA degradation and chalcone synthase A silencing in petunia

Article Abstract:

A model using Petunia plants bearing chalcone synthase A (chsA) transgenes is presented to illustrate how chsA RNA degradation is likely to be promoted to cause phenotypic cosuppression. It was observed that transgenic plants with purple or purple-white flowers can have high levels of endogene and transgene poly(A)+ chsA RNAs while plants with all-white flowers exhibit significant loss of endogene and transgene poly(A)+ RNAs. The results also indicated that the transgene RNA found in transgenic lines acts solely to trigger the induction of an existing chsA RNA-specific, posttranscriptional control mechanism.

Author: Cluster, P.D., Metzlaff, M., O'Dell, M., Flavell, R.B.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
Methods, Usage, Genetically modified plants, Polymerase chain reaction, RNA, Molecular genetics

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Association of fragile X syndrome with delayed replication of the FMR1 gene

Article Abstract:

The probable function of X inactivation imprinting fragile X syndrome is analyzed to examine the late replication construct for fragile regions, and many other X-related loci are studied to establish whether fragile X mutations change replication timing at significant distances from FMR1. The predictions of retarded replication of alleles from affected males are confirmed. Delayed replication was evident on both sides of the CGG repeat, suggesting that the retarded timing of replication is not the immediate outcome of the sole replication fork delaying at the expanded CGG repeat.

Author: Hansen, R. Scott, Canfield, Theresa K., Lamb, Mary M., Gartler, Stanley M., Laird, Charles D.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1993
DNA

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Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome

Article Abstract:

The three-dimensional solution structure of the K homology (KH) module is presented. The KH module is a sequence motif found in a number of proteins closely associated with RNA. The structure of the KH module shows a mixed alpha beta fold with a topology similar to the MuA transposase DNA-binding domain. The solved KH structure can provide valuable information on the effects of KH mutations in the fragile X mental retardation gene FMR1 as well as the site of RNA interaction.

Author: Musco, Giovanna, Stier, Gunter, Joseph, Catherine, Morelli, Maria Antonietta Castiglione, Nilges, Michael, Gibson, Toby J., Pastore, Annalisa
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
Chromosomal proteins

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Subjects list: Research, Analysis, Nucleotide sequence, Base sequence, Fragile X syndrome
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