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The proline-rich domain of MML-1 is biologically important but not required for localization to target promoters.


ABSTRACT: The only representative of the MYC superfamily transcription factors in C. elegans, MML-1 (Myc and Mondo-like 1), was shown to promote extended lifespan in a variety of models and to regulate some aspects of C. elegans development. This previous research did not involve molecular characterization of MML-1. Here we use available mml-1 mutant alleles and other reagents to demonstrate that MML-1 is modified by O-GlcNAc, binds to promoters of some genes directly regulated by the DOT-1.1 histone methyltransferase complex, and has a role in promoting neuronal migration. Surprisingly, we found that the deletion allele mml-1(ok849), which was considered a null, produces an internally truncated protein resulting from an in-frame deletion. Localization of this truncated product to MML-1 target promoters was not impaired. The deleted region of MML-1 is proline-rich, and its function is poorly understood in mammalian homologs of MML-1. Based on our work and previously published data we conclude that the internal proline-rich region of MML-1 is dispensable for DNA binding but is biologically important.

SUBMITTER: Ceballos A 

PROVIDER: S-EPMC8579147 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature

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The proline-rich domain of MML-1 is biologically important but not required for localization to target promoters.

Ceballos Ainhoa A   Esse Ruben R   Grishok Alla A  

microPublication biology 20211109


The only representative of the MYC superfamily transcription factors in <i>C. elegans</i>, MML-1 (Myc and Mondo-like 1), was shown to promote extended lifespan in a variety of models and to regulate some aspects of <i>C. elegans</i> development. This previous research did not involve molecular characterization of MML-1. Here we use available <i>mml-1</i> mutant alleles and other reagents to demonstrate that MML-1 is modified by <i>O</i>-GlcNAc, binds to promoters of some genes directly regulated  ...[more]

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