ZIB

Hits per page

hits 1 - 2 | 2 hits

Sorting

Electronic Resource

Conservation of the mammalian RNA polymerase II largest-subunit C-terminal domain (1992)

Barron-Casella, Emily ; Corden, Jeffry L.

Springer

Journal of molecular evolution 35 (1992), S. 405-410

add to mindlist on the mindlist

Details

ISSN: 1432-1432

Keywords: RNA polymerase II ; Largest subunit ; Carboxy-terminal domain ; Mammalian

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Summary We have isolated and sequenced a portion of the gene encoding the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II from three mammals. These mammalian sequences include one rodent and two primate CTDs. Comparisons of the new sequences to mouse and Chinese hamster show a high degree of conservation among the mammalian CTDs. Due to synonymous codon usage, the nucleotide differences between hamster, rat, ape, and human result in no amino acid changes. The amino acid sequence for the mouse CTD appears to have one different amino acid when compared to the other four sequences. Therefore, except for the one variation in mouse, all of the known mammalian CTDs have identical amino acid sequences. This is in marked contrast to the situation among more divergent species. The present study suggests that there is a strong evolutionary pressure to maintain the primary structure of the mammalian CTD.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00171818

Permalink

Library	Location	Call Number	Volume/Issue/Year	Availability

Others were also interested in ...

Paper (German National Licenses)

Fulltext

Electronic Resource

Quantitation of cap Z in conventional actin preparations and methods for further purification of actin (1995)

Casella, James F. ; Barron-Casella, Emily A. ; Torres, Michelle A.

New York, NY : Wiley-Blackwell

Cell Motility and the Cytoskeleton 30 (1995), S. 164-170

add to mindlist on the mindlist

Details

ISSN: 0886-1544

Keywords: actin ; purification ; methods ; kinetics ; Cap Z ; chickens ; antibodies ; blotting ; immuno-affinity purification ; immunoabsorbance ; muscle proteins ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: Gel-filtration is commonly used to remove contaminants from conventional actin prepared by the method of Spudich and Watt. It has been shown that this procedure removes the majority of a factor that reduces the low-shear viscosity of actin. We have previously reported that this factor is Cap Z, a barbed end capping protein. We now establish that, even after gel-filtration, enough Cap Z can be present in conventionally prepared actin to affect events occurring at the barbed ends of actin filaments. We also demonstrate that the concentration of Cap Z can be reduced to more than a log below the KD for binding of Cap Z to actin by either (1) immunoabsorbtion of conventionally prepared actin with anti-Cap Z antibodies, or (2) an additional cycle of polymerization/depolymerization followed by repeat gel-filtration. © 1995 Wiley-Liss, Inc.

Additional Material: 5 Ill.