ELAV proteins stabilize deadenylated intermediates in a novel in vitro mRNA deadenylation/degradation system

Article Abstract:

The ELAV family of ARE-binding proteins in vitro stabilize deadenylated intermediates acting in a novel messenger RNA (mRNA) deadenylation/degradation system. An in vitro mRNA stability system has been developed using exogenous polyadenylated RNA substrates and HeLa cell cytoplasmic S100 extracts. It reproduces regulated parts of mRNA decay. Addition of cold poly(A) competitor RNA activates a potent, ATP-dependent ribonucleolytic activity and a sequence-specific deadenylase activity in the extracts. Rates of degradation and deadenylation went up, affected by presence of various AU-rich elements in the body of substrate RNAs. It appears that mammal ELAV proteins help to regulate mRNA stability. They influence access of degradative enzymes to SNA substrates.

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Communication between Hin recombinase and Fis regulatory subunits during coordinate activation of Hin-catalyzed site-specific DNA inversion

Article Abstract:

The Hin DNA invertase is catalytically activated in being assembled into an invertasome complex that has two Fis dimers bound with an enhancer segment. Fis heterodimers with only one functional activating beta-arm are adequate to form catalytically competent invertasomes, although the two Fis dimers have to be able to activate Hin. A molecular model for the structure of invertasome has been proposed. The structure is consistent with available information about protein-DNA structures and shape of the DNA strands in the recombinant complex.

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Regulation of gene expression by TBP-associated proteins

Article Abstract:

TATA-binding protein (TBP), present in promoters used by RNA polymerases, is regulated in eukaryotes by a highly complex mechanism. Eight factors have been identified that interact with TBP: TAF(I)s, TAF(II)s, TAF(III)s, PTF/SNAPc, SAGA, Mot1, NC2 and Nots. The first four play a role in promoter selection, while the others work with TAF(II)s in regulation of expression of protein-coding genes. Negative regulation of TBP seems to be crucial.

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