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HSP90? plays an important role in piRNA biogenesis and retrotransposon repression in mouse.


ABSTRACT: HSP90, found in all kingdoms of life, is a major chaperone protein regulating many client proteins. We demonstrated that HSP90?, one of two paralogs duplicated in vertebrates, plays an important role in the biogenesis of fetal PIWI-interacting RNAs (piRNA), which act against the transposon activities, in mouse male germ cells. The knockout mutation of Hsp90? resulted in a large reduction in the expression of primary and secondary piRNAs and mislocalization of MIWI2, a PIWI homolog. Whereas the mutation in Fkbp6 encoding a co-chaperone reduced piRNAs of 28-32 nucleotides in length, the Hsp90? mutation reduced piRNAs of 24-32 nucleotides, suggesting the presence of both FKBP6-dependent and -independent actions of HSP90?. Although DNA methylation and mRNA levels of L1 retrotransposon were largely unchanged in the Hsp90? mutant testes, the L1-encoded protein was increased, suggesting the presence of post-transcriptional regulation. This study revealed the specialized function of the HSP90? isofom in the piRNA biogenesis and repression of retrotransposons during the development of male germ cells in mammals.

SUBMITTER: Ichiyanagi T 

PROVIDER: S-EPMC4231750 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature

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HSP90α plays an important role in piRNA biogenesis and retrotransposon repression in mouse.

Ichiyanagi Tomoko T   Ichiyanagi Kenji K   Ogawa Ayako A   Kuramochi-Miyagawa Satomi S   Nakano Toru T   Chuma Shinichiro S   Sasaki Hiroyuki H   Udono Heiichiro H  

Nucleic acids research 20140927 19


HSP90, found in all kingdoms of life, is a major chaperone protein regulating many client proteins. We demonstrated that HSP90α, one of two paralogs duplicated in vertebrates, plays an important role in the biogenesis of fetal PIWI-interacting RNAs (piRNA), which act against the transposon activities, in mouse male germ cells. The knockout mutation of Hsp90α resulted in a large reduction in the expression of primary and secondary piRNAs and mislocalization of MIWI2, a PIWI homolog. Whereas the m  ...[more]

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