The rel family of proteins
Article Abstract:
Rel proteins are pre-synthesized, inactive proteins who have at least 300 similar amino acid sequences in their amino terminals. They are found in the fruitfly Drosophila, the mammalian kappa gene transcription factor that binds to the kappa light chains of B lymphocytes, the turkey oncogenes and the proto-oncogene of many species. Rel proteins are essential in nuclear localization, nucleic acid binding and protein interactions subcellularly. These properties are mediated by the presence of a common nuclear targeting sequence and an arginine-arginine-X-serine phosphorylation site.
Publication Name: BioEssays
Subject: Biological sciences
ISSN: 0265-9247
Year: 1992
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The end of the message: 3'-end processing leading to polyadenylated messenger RNA
Article Abstract:
Processing of the 3'-end of messenger ribonucleic acids (mRNA) involves endonuclear primary transcript cleavage at the polyadenylate (polyA) tail and its polymerization. This requires the presence of the nucleotides AAUAAA, polyA polymerases, cleavage and polyadenylation factors, small nuclear ribonucleoprotein particles and other endonucleolytic cleavage factors. A variety of mRNA 3'-end polyadenylation processes exist across species.
Publication Name: BioEssays
Subject: Biological sciences
ISSN: 0265-9247
Year: 1992
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The prenylation of proteins
Article Abstract:
The oncogene product p21 (superscript ras), guanosine triphosphate binding proteins, nuclear lamins and heterometric G proteins undergo post-translational prenylation. This occurs through the binding of farnesyl or geranylgeranyl isoprenoids to the carboxyl terminal cysteine region by a thioether link. Prenylation is essential in membrane association processes, cell metabolism and growth and post-translational protein processing.
Publication Name: BioEssays
Subject: Biological sciences
ISSN: 0265-9247
Year: 1992
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