Nucleotide sequence of two actin genes of Lumbricus terrestris

doi:10.1016/0378-1119(96)00371-X

Gene

Volume 178, Issues 1–2, 1996, Pages 199-200

https://doi.org/10.1016/0378-1119(96)00371-X Get rights and content

Abstract

Two actin genes (actl-LUM and act2-LUM) of the annelid Lumbricus terrestris are characterised. Both genes reveal a single intron of 632 or 696 bp, respectively, located at exactly the same position. This intron position is currently the only intron position shared by some protostomic and most deuterostomic actin genes.

References (4)

T. Kusakabe et al.
Tunicate muscle actin genes
J. Mol. Biol.
(1992)
R.F. Doolittle
The multiplicity of domains in proteins
Ann. Rev. Biochem.
(1995)

There are more references available in the full text version of this article.

Cited by (1)

Four paralog gelsolin genes are differentially expressed in the earthworm Lumbricus terrestris
2017, Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology
Citation Excerpt :
However, it remains still questionable whether P1–P4 have specific subfunctions within the fast body wall and the slow gizzard muscle. Considering the existence of two actin isoforms in the earthworm (Lewke and Weber, 1996) and their likely differential expression it is conceivable that the distribution of EWAM proteins reflects a specific binding to different actin isoforms as it was shown for several other actin-binding proteins (De La Cruz, 2005; Larsson and Lindberg, 1988; Namba et al., 1992; Shuster et al., 1996; Tzima et al., 2000; Weber et al., 1992; Yao et al., 1996). On the other hand, the observed differences between EWAM P1–P4 could also reflect functional differences in binding to other actin binding proteins.
We have identified and characterized four distinct variants of the gelsolin-related protein (EWAM P1–P4) in the earthworm L. terrestris. All of these proteins biochemically qualify as gelsolins since they sever actin filaments in a calcium dependent manner. P1, P2 and P3 are present in the Lumbricus body wall muscle whereas in the gizzard muscle P3 and P4 were found. P1–P4 are encoded by four paralog genes and are differentially expressed in various muscle cell tissues. While the genes for P1 and P2 contain one intron, there was no intron in both P3 and P4 genes. The coding sequences consist of 1104 bp (368 amino acids) for P1/P4 and 1101 bp (367 amino acids) for P2/P3. Corresponding genes were confirmed by northern blot analysis which revealed three (calculated lengths: 3100, 2300 and 2100 nucleotides) and two (calculated lengths: 2300 and 1700 nucleotides) mRNA transcripts in the body wall and the gizzard, respectively. EWAM mRNA was localized by fluorescence in situ hybridization in the body wall and the gizzard muscle. P1 mRNA was detected in the inner proximal layers of both the circular and longitudinal muscle of the body wall whereas in the gizzard no significant staining was observed for P1. P2–P4 mRNAs were abundant in the outer distal layers of both the circular and the longitudinal muscles of both body wall and gizzard. The differential expression of four paralog gelsolin genes suggests a functional adaptation of different muscle cells with respect to actin filament turnover and modulation of its polymer state.

^☆: On request, the authors will supply detailed experimental evidence for the conclusions reached in this Short communication.

²: Present address: Max-Delbrück Laboratory, Carl von Linné Weg 10, D50829 Köln, Germany.

View full text

Short communicationNucleotide sequence of two actin genes of Lumbricus terrestris☆

Abstract

J. Mol. Biol.

The multiplicity of domains in proteins

Ann. Rev. Biochem.

Short communication
Nucleotide sequence of two actin genes of Lumbricus terrestris☆