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Biochemistry, Biophysics, and Structural Biology Commons

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Full-Text Articles in Biochemistry, Biophysics, and Structural Biology

Phospholipase C Of Clostridium Hemolyticum: Gene Characterization And Proof Of Its Role As A Protective Immunogen In Guinea Pigs , Paul Joseph Hauer Jan 2001

Phospholipase C Of Clostridium Hemolyticum: Gene Characterization And Proof Of Its Role As A Protective Immunogen In Guinea Pigs , Paul Joseph Hauer

Retrospective Theses and Dissertations

The phospholipase C (PLPC) gene from Clostridium hemolyticum was cloned using the polymerase chain reaction. An open reading frame which encodes a 399-amino acid protein, containing a 27-amino acid signal sequence, was identified. The molecular weight of the active protein was 42,869 daltons. A 16-amino acid N-terminal sequence determined by Edman degradation exactly matched the putative amino acid sequence of the gene product. Comparison of the nucleotide and amino acid sequences with Genebank databases demonstrated that the beta toxin of C. hemolyticum exhibits high homology with other bacterial PLPCs. The N-terminal portion of the beta toxin contains the zinc-binding ...


Molecular Mechanisms Of Cap And Poly(A) Independent Translation Of Barley Yellow Dwarf Virus Rna , Edwards M. Allen Jan 2001

Molecular Mechanisms Of Cap And Poly(A) Independent Translation Of Barley Yellow Dwarf Virus Rna , Edwards M. Allen

Retrospective Theses and Dissertations

Barley yellow dwarf virus RNA contains a translation element (3 'TE) that confers efficient cap-independent initiation at the 5 proximal AUG. Direct end-labeling of RNAs verified the absence of a 5 ' modification on virion RNA. Thus BYDV differs from related viruses by having neither a genome-linked protein nor a 5 ' cap. To function in the 3' UTR, the 3 'TE must recruit ribosomes and associated translation factors, and communicate with the 5' end of the mRNA where translation initiates. The communication function is mediated by direct base pairing between the 3'TE and the 5' UTR. We propose that protein ...