Open Access. Powered by Scholars. Published by Universities.®

Life Sciences Commons

Open Access. Powered by Scholars. Published by Universities.®

1994

Biology

Biological Sciences Faculty Research and Publications

Articles 1 - 2 of 2

Full-Text Articles in Life Sciences

A Small Family Of Elements With Long Inverted Repeats Is Located Near Sites Of Developmentally Regulated Dna Rearrangement In Tetrahymena Thermophila, John M. Wells, Jay Lee Edward Ellingson, Diana M. Catt, Patricia J. Berger, Kathleen M. Karrer Sep 1994

A Small Family Of Elements With Long Inverted Repeats Is Located Near Sites Of Developmentally Regulated Dna Rearrangement In Tetrahymena Thermophila, John M. Wells, Jay Lee Edward Ellingson, Diana M. Catt, Patricia J. Berger, Kathleen M. Karrer

Biological Sciences Faculty Research and Publications

Extensive DNA rearrangement occurs during the development of the somatic macronucleus from the germ line micronucleus in ciliated protozoans. The micronuclear junctions and the macronuclear product of a developmentally regulated DNA rearrangement in Tetrahymena thermophila, Tlr1, have been cloned. The intrachromosomal rearrangement joins sequences that are separated by more than 13 kb in the micronucleus with the elimination of moderately repeated micronucleus-specific DNA sequences. There is a long, 825-bp, inverted repeat near the micronuclear junctions. The inverted repeat contains two different 19-bp tandem repeats. The 19-bp repeats are associated with each other and with DNA rearrangements at seven locations …


The Mink Potassium Channel Exists In Functional And Nonfunctional Forms When Expressed In The Plasma Membrane Of Xenopus Oocytes, Edward M. Blumenthal, Leonard K. Kaczmarek May 1994

The Mink Potassium Channel Exists In Functional And Nonfunctional Forms When Expressed In The Plasma Membrane Of Xenopus Oocytes, Edward M. Blumenthal, Leonard K. Kaczmarek

Biological Sciences Faculty Research and Publications

The minK protein induces a slowly activating voltage-dependent potassium current when expressed in Xenopus oocytes. In order to measure the levels of minK protein in the plasma membrane, we have modified the minK gene by inserting a 9 amino acid epitope into the N- terminal domain of the protein sequence. When intact live oocytes are injected with the modified minK RNA and subsequently incubated with an antibody to this epitope, specific binding is detected, indicating that the N-terminal domain is extracellular. We found that when oocytes are injected with amounts of minK mRNA up to 50 ng, the levels of …