Structure and function of unidecapeptide in the poly(A) binding protein.
We have shown that a synthetic unidecapeptide bound to poly(A) stimulated mRNA (poly A)+ [Rubin & Halim (1993), Biochemistry and Mol. Biol. Int. 31,267-278]. We further examined the structure of the unidecapeptide by circular dichroism spectroscopy and found it to be beta-sheet. Furthermore, the synthetic peptide was found to shorten and lengthen the poly(A) tail at the 3' end of rabbit globin mRNA. The shortening of the poly(A) tail was caused by a hexamer [K (or R)GFGFV], while the lengthening of the poly(A) tail was stimulated by the GKS sequence.
Rubin
H N
HN
San Diego Institute of Molecular Biology and Structural RNA, CA 92121.
Halim
M N
MN
D000595:Amino Acid Sequence; D000818:Animals; D002942:Circular Dichroism; D005914:Globins / Q000235:genetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry / Q000378:metabolism; D011061:Poly A / Q000378:metabolism*; D039102:Poly(A)-Binding Proteins; D017433:Protein Structure, Secondary; D012333:RNA, Messenger / Q000737:chemistry / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D011817:Rabbits
D009842:Oligopeptides; D039102:Poly(A)-Binding Proteins; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D011061:Poly A; D005914:Globins