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Biomedical subjects

D Gallwitz

Publications and source records attributed to D Gallwitz.

104 records · Page 6Linked to original sources
PubMed1969

Histone synthesis in vitro by cytoplasmic microsomes from HeLa cells.

HeLa cell microsomes incorporate labeled amino acids in vitro into acid-soluble proteins which have the same electrophoretic mobility as histones isolated from tile purified HeLa cell nuclei. The capacity to Svnthesize histones in vitro is dependent on deoxyribonucleic acid synthesis in the cells from which the microsonal fraction is prepared.

Arginine↗
PubMedDate not supplied

A yeast gene encoding a protein homologous to the human c-has/bas proto-oncogene product.

Organisms amenable to easy genetic analysis should prove helpful in assessing the function of at least those proto-oncogene products which are highly conserved in different eukaryotic cells. One obvious possibility is to pursue the matter in Drosophila melanogaster DNA, which has sequences homologous to several vertebrate oncogenes. Another is to turn to the yeast Saccharomyces cerevisiae, if it contains proto-oncogene sequences. Here we report the identification of a gene in S. cerevisiae which codes for a 206 amino acid protein (YP2) that exhibits striking homology to the p21 products of the human c-has/bas proto-oncogenes and the transforming p21 proteins of the Harvey (v-rasH) and Kirsten (v-rasK) murine sarcoma viral oncogenes. The YP2 gene is located between the actin and the tubulin gene on chromosome VI and is expressed in growing cells. The protein it encodes might share the nucleotide-binding capacity of p21 proteins.

Actins↗
PubMedDate not supplied

Msb4p, a protein involved in Cdc42p-dependent organization of the actin cytoskeleton, is a Ypt/Rab-specific GAP.

Ypt/Rab proteins of the Ras superfamily are regulators of protein transport in exo- and endocytosis. Like Ras and Rho proteins, they have a slow intrinsic GTPase activity that can be accelerated by several orders of magnitude by GTPase-activating proteins (GAP). Here we describe a new member of a family of Ypt/Rab-specific GAPs, Msb4p/Gyp4p, that shares with other Gyp family members significant homology in the catalytic domain, recently identified in Gyp1p and Gyp7p. Purified Msb4p/Gyp4p acts primarily on Sec4p, Ypt6p and Ypt7p and might have a role in polarized secretion.

Actins↗