Variable and constant regions in the C‐terminus of vinculin and metavinculin
Open Access
- 15 February 1993
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 317 (3) , 189-194
- https://doi.org/10.1016/0014-5793(93)81274-4
Abstract
Metavinculin differs from vinculin in having an additional insert of 68 to 79 amino acids in length in the C‐tenninal half of the molecule. Cross‐species comparison of metavinculin sequences from pig, man, chicken and frog reveals a division of the insert into two parts: the first variable and the second highly conserved. The longest insert, 79 amino acids, was found in Xenopus laevis. Three different C‐terminal constructs of vinculin and metavinculin over‐expressed in E. coli could be purified by column chromatography. Two‐dimensional gel electrophoresis and peptide analysis revealed pI values between 8.35 and 10.25 for the recombinant proteins. Biochemical and structural features of the metavinculin‐specific sequence and the conserved vinculin/metavinculin carboxy‐terminus are discussed.Keywords
This publication has 30 references indexed in Scilit:
- Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genesPublished by Elsevier ,2004
- An additional exon in the human vinculin gene specifically encodes meta‐vinculin‐specific difference peptideEuropean Journal of Biochemistry, 1992
- The cytoplasmic domain of adherens‐type junctionsCell Motility, 1991
- Paxillin: a new vinculin-binding protein present in focal adhesions.The Journal of cell biology, 1990
- Identification of a talin binding site in the cytoskeletal protein vinculin.The Journal of cell biology, 1989
- Meta‐vinculin distribution in adult human tissues and cultured cellsFEBS Letters, 1986
- Meta-vinculin—a vinculin-related protein with solubility properties of a membrane proteinNature, 1982
- Isolation of biologically active ribonucleic acid from sources enriched in ribonucleaseBiochemistry, 1979
- Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteinsJournal of Molecular Biology, 1978
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970