A lasp family protein of Ciona intestinalis.
Lasp-1 and lasp-2 are actin-binding proteins that contain a LIM domain, nebulin repeats, and an SH3 domain and they are significantly conserved in mammalian and avian. Lasp-1 is widely expressed in nonmuscle tissues and lasp-2 is specifically expressed in the brain. Genes encoding proteins homologous to lasp-1 and lasp-2 were deposited in the genome/cDNA database of invertebrates such as sea urchins, nematodes, and insects; however, function of their proteins have not been studied in detail. In this study, we analyzed the gene structure, actin-binding activity, and expression of the lasp protein of the ascidian Ciona intestinalis (Ci lasp). A single gene encoding lasp protein was found in the ascidian, and the amino acid sequences of Ci lasp and other invertebrate lasp proteins exhibited similarity to vertebrate lasp-1 and lasp-2 to the same extent. A part of the exon-intron boundaries was conserved between the vertebrate lasp-1, the vertebrate lasp-2 and the invertebrate lasp genes. Ci lasp exhibited actin-binding activity in a co-sedimentation assay. In situ hybridization revealed that the expression of Ci lasp mRNA was apparent in nervous system of early embryos and was detected in various tissues in young adults. This suggests that the functions of invertebrate lasp proteins might include the functions of vertebrate lasp-1 and lasp-2.
Terasaki
Asako G
AG
Graduate School of Science and Technology, Chiba University, Chiba 263-8522, Japan. saki@mail.ne.jp
Hiruta
Jin
J
Suzuki
Junko
J
Sakamoto
Sachiko
S
Nishioka
Tatsuji
T
Suzuki
Hiroshi
H
Ohashi
Kazuyo
K
Azumi
Kaoru
K
Ogasawara
Michio
M
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002938:Ciona intestinalis / Q000196:embryology / Q000235:genetics* / Q000378:metabolism*; D003001:Cloning, Molecular; D017931:DNA Primers / Q000235:genetics; D005260:Female; D015870:Gene Expression; D017403:In Situ Hybridization; D008297:Male; D008840:Microfilament Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D020411:Oligonucleotide Array Sequence Analysis; D010802:Phylogeny; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D018909:src Homology Domains
D017931:DNA Primers; D008840:Microfilament Proteins; D011994:Recombinant Proteins