A Novel Family of Unconventional Actins in Volvocalean Algae

Overview

Journal J Mol Evol

Specialty Biochemistry

Date 2004 Jan 24

PMID 14738314

Citations 5

Authors

Takako Kato-Minoura

Masayo Okumura

Masafumi Hirono

Ritsu Kamiya

Affiliations

Soon will be listed here.

Abstract

The unicellular green alga Chlamydomonas reinhardtii has two actin genes, one encoding a conventional actin (90% amino acid identity with mammalian actin), the other a highly divergent actin (64% identity) named novel actin-like protein (NAP). To see whether the presence of conventional and unconventional actins in a single organism is unique to C. reinhardtii, we searched for genomic sequences related to the NAP sequence in several other species of volvocalean algae. Here we show that Chlamydomonas moewusii and Volvox carteri also have, in addition to a conventional actin, an unconventional actin similar to the C. reinhardtii NAP. Analyses of the deduced protein sequences indicated that the NAP homologues form a distinct group derived from conventional actin.

Citing Articles

Composition and function of ciliary inner-dynein-arm subunits studied in Chlamydomonas reinhardtii.

Yamamoto R, Hwang J, Ishikawa T, Kon T, Sale W Cytoskeleton (Hoboken). 2021; 78(3):77-96.

PMID: 33876572 PMC: 8217317. DOI: 10.1002/cm.21662.

The Chlamydomonas cell cycle.

Cross F, Umen J Plant J. 2015; 82(3):370-392.

PMID: 25690512 PMC: 4409525. DOI: 10.1111/tpj.12795.

The actin multigene family of Paramecium tetraurelia.

Sehring I, Mansfeld J, Reiner C, Wagner E, Plattner H, Kissmehl R BMC Genomics. 2007; 8:82.

PMID: 17391512 PMC: 1852557. DOI: 10.1186/1471-2164-8-82.

Tempo and mode of spliceosomal intron evolution in actin of foraminifera.

Flakowski J, Bolivar I, Fahrni J, Pawlowski J J Mol Evol. 2006; 63(1):30-41.

PMID: 16755352 DOI: 10.1007/s00239-005-0061-z.

Giardia lamblia behavior under cytochalasins treatment.

Correa G, Benchimol M Parasitol Res. 2005; 98(3):250-6.

PMID: 16344997 DOI: 10.1007/s00436-005-0065-z.

References

Weber K, Kabsch W . Intron positions in actin genes seem unrelated to the secondary structure of the protein. EMBO J. 1994; 13(6):1280-6. PMC: 394942. DOI: 10.1002/j.1460-2075.1994.tb06380.x. View

Uryu S, Hirono M, Kamiya R . Highly divergent actin expressed in a Chlamydomonas mutant lacking the conventional actin gene. Biochem Biophys Res Commun. 1998; 251(1):71-6. DOI: 10.1006/bbrc.1998.9373. View

Goodson H, Hawse W . Molecular evolution of the actin family. J Cell Sci. 2002; 115(Pt 13):2619-22. DOI: 10.1242/jcs.115.13.2619. View

Sugase Y, Hirono M, Kindle K, Kamiya R . Cloning and characterization of the actin-encoding gene of Chlamydomonas reinhardtii. Gene. 1996; 168(1):117-21. DOI: 10.1016/0378-1119(95)00711-3. View

Schafer D, Schroer T . Actin-related proteins. Annu Rev Cell Dev Biol. 1999; 15:341-63. DOI: 10.1146/annurev.cellbio.15.1.341. View

Larson A, Kirk M, Kirk D . Molecular phylogeny of the volvocine flagellates. Mol Biol Evol. 1992; 9(1):85-105. DOI: 10.1093/oxfordjournals.molbev.a040710. View

Jones D, Taylor W, Thornton J . The rapid generation of mutation data matrices from protein sequences. Comput Appl Biosci. 1992; 8(3):275-82. DOI: 10.1093/bioinformatics/8.3.275. View

Cresnar B, Mages W, Muller K, Salbaum J, Schmitt R . Structure and expression of a single actin gene in Volvox carteri. Curr Genet. 1990; 18(4):337-46. DOI: 10.1007/BF00318215. View

Miller S, Schmitt R, Kirk D . Jordan, an active Volvox transposable element similar to higher plant transposons. Plant Cell. 1993; 5(9):1125-38. PMC: 160346. DOI: 10.1105/tpc.5.9.1125. View

10.

Hepperle D, Nozaki H, Hohenberger S, Huss V, Morita E, Krienitz L . Phylogenetic position of the Phacotaceae within the Chlamydophyceaeas revealed by analysis of 18S rDNA and rbcL sequences. J Mol Evol. 1998; 47(4):420-30. DOI: 10.1007/pl00006399. View

11.

Kato T, Kagami O, Yagi T, Kamiya R . Isolation of two species of Chlamydomonas reinhardtii flagellar mutants, ida5 and ida6, that lack a newly identified heavy chain of the inner dynein arm. Cell Struct Funct. 1993; 18(6):371-7. DOI: 10.1247/csf.18.371. View

12.

Piperno G, Luck D . An actin-like protein is a component of axonemes from Chlamydomonas flagella. J Biol Chem. 1979; 254(7):2187-90. View

13.

Hirono M, Uryu S, Ohara A, Kato-Minoura T, Kamiya R . Expression of conventional and unconventional actins in Chlamydomonas reinhardtii upon deflagellation and sexual adhesion. Eukaryot Cell. 2003; 2(3):486-93. PMC: 161444. DOI: 10.1128/EC.2.3.486-493.2003. View

14.

Ina Y . New methods for estimating the numbers of synonymous and nonsynonymous substitutions. J Mol Evol. 1995; 40(2):190-226. DOI: 10.1007/BF00167113. View

15.

Gorman D, Levine R . Cytochrome f and plastocyanin: their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardi. Proc Natl Acad Sci U S A. 1965; 54(6):1665-9. PMC: 300531. DOI: 10.1073/pnas.54.6.1665. View

16.

Cavalier-Smith T . The number of symbiotic origins of organelles. Biosystems. 1992; 28(1-3):91-106; discussion 107-8. DOI: 10.1016/0303-2647(92)90011-m. View

17.

Lee V, Finstad S, Huang B . Cloning and characterization of a gene encoding an actin-related protein in Chlamydomonas. Gene. 1997; 197(1-2):153-9. DOI: 10.1016/s0378-1119(97)00254-0. View

18.

Weeks D, Beerman N, Griffith O . A small-scale five-hour procedure for isolating multiple samples of CsCl-purified DNA: application to isolations from mammalian, insect, higher plant, algal, yeast, and bacterial sources. Anal Biochem. 1986; 152(2):376-85. DOI: 10.1016/0003-2697(86)90423-9. View

19.

Thompson J, Higgins D, Gibson T . CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994; 22(22):4673-80. PMC: 308517. DOI: 10.1093/nar/22.22.4673. View

20.

Stibitz T, Keeling P, Bhattacharya D . Symbiotic origin of a novel actin gene in the cryptophyte Pyrenomonas helgolandii. Mol Biol Evol. 2000; 17(11):1731-8. DOI: 10.1093/oxfordjournals.molbev.a026271. View