| pubmed-article:1633812 | pubmed:abstractText | Systematic analysis of soluble proteins in developing rat cerebellum by an automated two-dimensional liquid-chromatography system detected a number of proteins which increased transiently during the initial stage of postnatal development. One of the proteins, V-1, was isolated using a liquid-chromatography system, and its amino acid sequence was determined by analysis of the purified protein. The sequence showed that the V-1 protein consists of 117 amino acids with an acetylated N-terminus, and has 2.5 internal sequence repeats of 33 amino acids. Computer retrieval of the sequence indicated that the repeated sequences have a structural characteristics of the cdc10/SWI6 motif, which is found in a series of proteins, including those involved in cell-cycle control and cell-fate determination in yeast, Drosophila melanogaster and Caenorhabditis elegans. The structure of V-1, coupled with its controlled expression in early postnatal development, implies a potential role for V-1 in cerebellar morphogenesis. | lld:pubmed |
