Dissecting the structural basis of MEIG1 interaction with PACRG.

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 Rep

journal_title

Scientific reports

authors

Li W,Walavalkar NM,Buchwald WA,Teves ME,Zhang L,Liu H,Bilinovich S,Peterson DL,Strauss JF 3rd,Williams DC Jr,Zhang Z

doi

10.1038/srep18278

subject

Has Abstract

pub_date

2016-01-04 00:00:00

pages

18278

issn

2045-2322

pii

srep18278

journal_volume

6

pub_type

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