New class of blue animal pigments based on Frizzled and Kringle protein domains.
The nature of coloration in many marine animals remains poorly investigated. Here we studied the blue pigment of a scyfoid jellyfish Rhizostoma pulmo and determined it to be a soluble extracellular 30-kDa chromoprotein with a complex absorption spectrum peaking at 420, 588, and 624 nm. Furthermore, we cloned the corresponding cDNA and confirmed its identity by immunoblotting and mass spectrometry experiments. The chromoprotein, named rpulFKz1, consists of two domains, a Frizzled cysteine-rich domain and a Kringle domain, inserted into one another. Generally, Frizzleds are members of a basic Wnt signal transduction pathway investigated intensely with regard to development and cancerogenesis. Kringles are autonomous structural domains found throughout the blood clotting and fibrinolytic proteins. Neither Frizzled and Kringle domains association with any type of coloration nor Kringle intrusion into Frizzled sequence was ever observed. Thus, rpulFKz1 represents a new class of animal pigments, whose chromogenic group remains undetermined. The striking homology between a chromoprotein and members of the signal transduction pathway provides a novel node in the evolution track of growth factor-mediated morphogenesis compounds.
Bulina
Maria E
ME
Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, 117997 Moscow.
Lukyanov
Konstantin A
KA
Yampolsky
Ilia V
IV
Chudakov
Dmitry M
DM
Staroverov
Dmitry B
DB
Shcheglov
Alexander S
AS
Gurskaya
Nadya G
NG
Lukyanov
Sergey
S
D000595:Amino Acid Sequence; D000818:Animals; D018082:Kringles / Q000502:physiology*; D008164:Luminescent Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010860:Pigments, Biological / Q000302:isolation & purification; D037401:Scyphozoa / Q000737:chemistry*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013053:Spectrophotometry
D008164:Luminescent Proteins; D010860:Pigments, Biological