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A novel type of crystallin in the frog eye lens
Author(s) -
Tomarev Stanislav I.,
Zinovieva Rina D.,
Dolgilevich Svetlana M.,
Luchin Sergey V.,
Krayev Alexander S.,
Skryabin Konstantin G.,
Gause Georgyi G.
Publication year - 1984
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(84)80508-6
Subject(s) - polyadenylation , nucleotide , biology , nucleic acid sequence , coding region , crystallin , open reading frame , sequence (biology) , eye lens , peptide sequence , lens (geology) , genetics , dna , messenger rna , gene , paleontology
The nucleotide sequence of a cloned DNA coding for the 35‐kDa polypeptide of the eye lens of the frog Rana temporaria has been determined. The sequence without connectors and poly(A) tract is 889 nucleotides in length and shows no homology with sequences coding for other classes of crystallins; α‐, β‐, γ‐ or δ‐crystallins. The sequence contains one reading frame 675 nucleotides in length, an apparently intact 3′‐non‐translated region with the polyadenylation signal sequence and a poly(A) tract; the 5′‐non‐ translated region is lost along with part of the coding region; this accounts for about 1/4 of the total mRNA length. The secondary structure prediction according to the Ptitsin‐Finkelstein method shows the presence of predominantly β‐strands with only a few α‐helical regions. We conclude that the 35‐kDa polypeptide from the frog eye lens belongs to a new class of eye lens crystallins for which we propose the name ϵ‐crystallin.