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Structural insight into the central element assembly of the synaptonemal complex.

Lu J, Gu Y, Feng J, Zhou W, Yang X, Shen Y - Sci Rep (2014)

Bottom Line: Our studies show that functional SYCE3 most likely forms a dimer or higher order oligomer in cells.Furthermore, we demonstrate that the SYCE3 N-helix interacts with the SYCE1 C-helix, which is another central element component.Our results suggest that helical packing may mediate intra- or inter-association of each central element protein component, thereby playing an essential role in forming the synaptonemal complex central elements.

View Article: PubMed Central - PubMed

Affiliation: 1] State Key Laboratory of Medicinal Chemical Biology, Nankai University, 94 Weijin Road, Tianjin 300071, China [2] College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China.

ABSTRACT
The key step in meiosis is synaptonemal complex formation, which mediates homologous chromosome alignment and synapsis. False pairing between homologous chromosomes produces infertility. Here, we present a crystal structure of the mouse meiosis-specific protein SYCE3, which is a component of the synaptonemal complex central element. Our studies show that functional SYCE3 most likely forms a dimer or higher order oligomer in cells. Furthermore, we demonstrate that the SYCE3 N-helix interacts with the SYCE1 C-helix, which is another central element component. Our results suggest that helical packing may mediate intra- or inter-association of each central element protein component, thereby playing an essential role in forming the synaptonemal complex central elements.

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Related in: MedlinePlus

Interactions between SYCE3 and SYCE1.(A) COS-7 cells were transfected with Myc-SYCE1 and the respective full-length SYCE3, SYCE3 N-helix, and SYCE3 C-helix EGFP fusion constructs. Myc-SYCE1 can bind the full-length SYCE3 and SYCE3 N-helix. The SYCE3 C-helix does not bind SYCE1. (B) COS-7 cells were transfected with EGFP-SYCE3 and the respective Myc fusion constructs composed of full-length SYCE1 and SYCE1 without C-helix. The results show that SYCE1 without the C-helix does not bind SYCE3. Full-length blots/gels are presented in Supplementary Figure 1.
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f3: Interactions between SYCE3 and SYCE1.(A) COS-7 cells were transfected with Myc-SYCE1 and the respective full-length SYCE3, SYCE3 N-helix, and SYCE3 C-helix EGFP fusion constructs. Myc-SYCE1 can bind the full-length SYCE3 and SYCE3 N-helix. The SYCE3 C-helix does not bind SYCE1. (B) COS-7 cells were transfected with EGFP-SYCE3 and the respective Myc fusion constructs composed of full-length SYCE1 and SYCE1 without C-helix. The results show that SYCE1 without the C-helix does not bind SYCE3. Full-length blots/gels are presented in Supplementary Figure 1.

Mentions: A previous report indicated that SYCE3 co-localizes with SYCE1 and aids in recruiting SYCE1 to SYCP116; thus, we performed co-IP experiments to further study the interaction between SYCE3 and SYCE1. To examine which SYCE3 helix interacts with SYCE1, we co-transfected constructs encoding EGFP-tagged fusion proteins composed of the full-length SYCE3, SYCE3 N-helix (aa1-52), or SYCE3 C-helix (aa 53–88) and a construct encoding Myc-tagged SYCE1 into COS-7 cells. Our data show that both the full-length SYCE3 and SYCE3 N-helix interacts with SYCE1; however, we did not detect an interaction between the SYCE3 C-helix and SYCE1 (Figure 3A).


Structural insight into the central element assembly of the synaptonemal complex.

Lu J, Gu Y, Feng J, Zhou W, Yang X, Shen Y - Sci Rep (2014)

Interactions between SYCE3 and SYCE1.(A) COS-7 cells were transfected with Myc-SYCE1 and the respective full-length SYCE3, SYCE3 N-helix, and SYCE3 C-helix EGFP fusion constructs. Myc-SYCE1 can bind the full-length SYCE3 and SYCE3 N-helix. The SYCE3 C-helix does not bind SYCE1. (B) COS-7 cells were transfected with EGFP-SYCE3 and the respective Myc fusion constructs composed of full-length SYCE1 and SYCE1 without C-helix. The results show that SYCE1 without the C-helix does not bind SYCE3. Full-length blots/gels are presented in Supplementary Figure 1.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4231325&req=5

f3: Interactions between SYCE3 and SYCE1.(A) COS-7 cells were transfected with Myc-SYCE1 and the respective full-length SYCE3, SYCE3 N-helix, and SYCE3 C-helix EGFP fusion constructs. Myc-SYCE1 can bind the full-length SYCE3 and SYCE3 N-helix. The SYCE3 C-helix does not bind SYCE1. (B) COS-7 cells were transfected with EGFP-SYCE3 and the respective Myc fusion constructs composed of full-length SYCE1 and SYCE1 without C-helix. The results show that SYCE1 without the C-helix does not bind SYCE3. Full-length blots/gels are presented in Supplementary Figure 1.
Mentions: A previous report indicated that SYCE3 co-localizes with SYCE1 and aids in recruiting SYCE1 to SYCP116; thus, we performed co-IP experiments to further study the interaction between SYCE3 and SYCE1. To examine which SYCE3 helix interacts with SYCE1, we co-transfected constructs encoding EGFP-tagged fusion proteins composed of the full-length SYCE3, SYCE3 N-helix (aa1-52), or SYCE3 C-helix (aa 53–88) and a construct encoding Myc-tagged SYCE1 into COS-7 cells. Our data show that both the full-length SYCE3 and SYCE3 N-helix interacts with SYCE1; however, we did not detect an interaction between the SYCE3 C-helix and SYCE1 (Figure 3A).

Bottom Line: Our studies show that functional SYCE3 most likely forms a dimer or higher order oligomer in cells.Furthermore, we demonstrate that the SYCE3 N-helix interacts with the SYCE1 C-helix, which is another central element component.Our results suggest that helical packing may mediate intra- or inter-association of each central element protein component, thereby playing an essential role in forming the synaptonemal complex central elements.

View Article: PubMed Central - PubMed

Affiliation: 1] State Key Laboratory of Medicinal Chemical Biology, Nankai University, 94 Weijin Road, Tianjin 300071, China [2] College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China.

ABSTRACT
The key step in meiosis is synaptonemal complex formation, which mediates homologous chromosome alignment and synapsis. False pairing between homologous chromosomes produces infertility. Here, we present a crystal structure of the mouse meiosis-specific protein SYCE3, which is a component of the synaptonemal complex central element. Our studies show that functional SYCE3 most likely forms a dimer or higher order oligomer in cells. Furthermore, we demonstrate that the SYCE3 N-helix interacts with the SYCE1 C-helix, which is another central element component. Our results suggest that helical packing may mediate intra- or inter-association of each central element protein component, thereby playing an essential role in forming the synaptonemal complex central elements.

Show MeSH
Related in: MedlinePlus