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Proline‐ and alanine‐rich N‐terminal extension of the basic bovine β‐crystallin B 1 chains
Author(s) -
Berbers G.A.M.,
Hoekman W.A.,
Bloemendal H.,
de Jong W.W.,
Kleinschmidt T.,
Braunitzer G.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)81013-8
Subject(s) - beta (programming language) , proline , peptide sequence , alanine , chemistry , protein primary structure , sequence (biology) , amino acid , stereochemistry , biochemistry , gene , computer science , programming language
The amino acid sequence of the N‐terminal region of the two basic bovine β‐crystallin B 1 chains has been analyzed. The results reveal that βB 1b is derived in vivo from the primary gene product βB 1a by removal of a short N‐terminal sequence. It appears that the βB 1 chains have the same domain structure as observed in other β‐ and γ‐crystallin chains. They have, however, a very long N‐terminal extension in comparison with other β‐chains. This extension is mainly composed of a remarkable Pro‐ and Ala‐rich sequence, which suggests an interaction of these structural proteins with the cytoskeleton and/or the plasma membranes of the lens cells.