Dissecting the structural basis of MEIG1 interaction with PACRG

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 ass...

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Bibliographic Details
Published in:Scientific reports 2016-01, Vol.6 (1), p.18278-18278, Article 18278
Main Authors: Li, Wei, Walavalkar, Ninad M., Buchwald, William A., Teves, Maria E., Zhang, Ling, Liu, Hong, Bilinovich, Stephanie, Peterson, Darrell L., Strauss III, Jerome F., Williams Jr, David C., Zhang, Zhibing
Format: Article
Language:English
Subjects:
140/131
38/1
38/70
631/535/878/1263
631/80/470/1981
82/83
Amino Acid Sequence
Amino acids
Animals
Cell Cycle Proteins - chemistry
Cell Cycle Proteins - genetics
Cell Cycle Proteins - metabolism
Flagella
Humanities and Social Sciences
Hydrophobicity
Meiosis
Mice
Models, Molecular
Molecular Sequence Data
multidisciplinary
Mutation
Nuclear Magnetic Resonance, Biomolecular
Nuclear Proteins - chemistry
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Parkin protein
Phosphoproteins - chemistry
Phosphoproteins - genetics
Phosphoproteins - metabolism
Protein Binding
Protein Conformation
Protein Folding
Protein Stability
Proteins - chemistry
Proteins - genetics
Proteins - metabolism
Recombinant Proteins
Science
Solvents
Sperm
Spermatids
Spermatocytes
Structure-Activity Relationship
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Summary: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.
ISSN:2045-2322
2045-2322
DOI:10.1038/srep18278