Abstract:
:The product of the meiosis-expressed gene 1 (MEIG1) is found in the cell bodies of spermatocytes and recruited to the manchette, a structure unique to elongating spermatids, by Parkin co-regulated gene (PACRG). This complex is essential for targeting cargo to the manchette during sperm flagellum assembly. Here we show that MEIG1 adopts a unique fold that provides a large surface for interacting with other proteins. We mutated 12 exposed and conserved amino acids and show that four of these mutations (W50A, K57E, F66A, Y68A) dramatically reduce binding to PACRG. These four amino acids form a contiguous hydrophobic patch on one end of the protein. Furthermore, each of these four mutations diminishes the ability of MEIG1 to stabilize PACRG when expressed in bacteria. Together these studies establish the unique structure and key interaction surface of MEIG1 and provide a framework to explore how MEIG1 recruits proteins to build the sperm tail.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Li W,Walavalkar NM,Buchwald WA,Teves ME,Zhang L,Liu H,Bilinovich S,Peterson DL,Strauss JF 3rd,Williams DC Jr,Zhang Zdoi
10.1038/srep18278subject
Has Abstractpub_date
2016-01-04 00:00:00pages
18278issn
2045-2322pii
srep18278journal_volume
6pub_type
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