Dataset Information

Phylo-proteomics Reveals Conserved Patterns of Axonemal Dynein Methylation Across the Motile Ciliated Eukaryotes (addendum)

ABSTRACT: Assembly of the axonemal dynein motors that power ciliary motility occurs in the cytoplasm. Studies in a broad array of organisms have revealed that at least nineteen cytosolic factors are specifically required for this process. Recently, one of these factors (DNAAF3/PF22) was identified as an S-adenosylmethionine-dependent methyltransferase. Furthermore, examination of dyneins from the green alga Chlamydomonas found that axonemal dyneins are methylated at sub-stoichiometric levels on multiple sites including key Lys and Arg residues in several of the nucleotide binding domains and on the microtubule-binding region. Given the highly conserved nature of axonemal dyneins and their cytoplasmic assembly factors, one key question is whether methylation is exclusively present only in dyneins from the chlorophyte algae, or if these modifications occur more broadly throughout the motile ciliated eukaryotes. Here we take a phylo-proteomic approach and examine dynein methylation in a wide range of eukaryotic organisms bearing motile cilia. We find unambiguous evidence for methylation of axonemal dyneins in alveolates, chlorophytes, trypanosomes, and throughout most of the metazoa, including ctenophores, echinoderms, mollusks, ascidians, and vertebrates. Intriguingly, we were unable to identify a single instance of methylation on Drosophila sperm dynein even though dipterans express a Dnaaf3 ortholog, or in spermatozoids of the fern Ceratopteris which assembles inner arms but lacks both outer arm dyneins and DNAAF3. Thus, methylation is a post-translational feature of axonemal dyneins that has been broadly conserved in most eukaryotic groups suggesting the existence of a post-translational dynein code that variably modifies the function of these motors.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Chlamydomonas Sp. Hs-5 Drosophila Willistoni

TISSUE(S): Ciliary Body

SUBMITTER: Jeremy Balsbaugh

LAB HEAD: Jeremy Balsbaugh

PROVIDER: PXD058873 | Pride | 2025-02-20

REPOSITORIES: pride

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Dataset's files

Source:

			Action	DRS
	20241004_AxovsMM_Chlamy_txt.zip	Other
	20241004_jlb_MAntoku_King_CC125axo_tryp_500ng_60min_OTOThcd_Wat25cmBEH_1.raw	Raw
	20241004_jlb_MAntoku_King_CC125mm_tryp_500ng_60min_OTOThcd_Wat25cmBEH_1.raw	Raw
	20241004_jlb_MAntoku_King_pf22axo_tryp_500ng_60min_OTOThcd_Wat25cmBEH_1.raw	Raw
	20241004_jlb_MAntoku_King_pf22mm_tryp_500ng_60min_OTOThcd_Wat25cmBEH_1.raw	Raw

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Publications

Phyloproteomics Reveals Conserved Patterns of Axonemal Dynein Methylation Across the Motile Ciliated Eukaryotes.

Sakato-Antoku Miho M Patel Nikisha N Inaba Mayu M Rao Qinhui Q Yang Jun J Patel-King Ramila S RS Inaba Kazuo K Balsbaugh Jeremy L JL King Stephen M SM

Molecular biology of the cell 20250219

Axonemal dynein assembly occurs in the cytoplasm and numerous cytosolic factors are specifically required for this process. Recently, one factor (DNAAF3/PF22) was identified as a methyltransferase. Examination of <i>Chlamydomonas</i> dyneins found they are methylated at sub-stoichiometric levels on multiple sites, including Lys and Arg residues in several of the nucleotide binding domains and on the microtubule-binding region. Given the highly conserved nature of axonemal dyneins, one key questi ...[more]

PMID: 39969973

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