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Review
. 2024 Feb 28;52(1):379-393.
doi: 10.1042/BST20230712.

The molecular machinery of meiotic recombination

Linda Chen  1 , John R Weir  1
Affiliations
Review

The molecular machinery of meiotic recombination

Linda Chen et al. Biochem Soc Trans. .

Abstract

Meiotic recombination, a cornerstone of eukaryotic diversity and individual genetic identity, is essential for the creation of physical linkages between homologous chromosomes, facilitating their faithful segregation during meiosis I. This process requires that germ cells generate controlled DNA lesions within their own genome that are subsequently repaired in a specialised manner. Repair of these DNA breaks involves the modulation of existing homologous recombination repair pathways to generate crossovers between homologous chromosomes. Decades of genetic and cytological studies have identified a multitude of factors that are involved in meiotic recombination. Recent work has started to provide additional mechanistic insights into how these factors interact with one another, with DNA, and provide the molecular outcomes required for a successful meiosis. Here, we provide a review of the recent developments with a focus on protein structures and protein-protein interactions.

Keywords: DNA replication and recombination; chromosomes; meiosis.

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Conflict of interest statement

The authors declare that there are no competing interests associated with the manuscript.

Figures

Figure 1.
Figure 1.. Overview of the key stages in meiosis.
(A) Cartoon overview of meiosis in the context of the generation and continuation of eukaryotic life. On the right-hand side, cartoon chromosomes are considered to be homologues. The stages of meiosis I are shown as DSB formation, crossover formation and the segregation of homologues. The outcome of meiosis II is shown at the bottom as four genetically distinct haploid gametes. (B) Inset of meiotic DSB formation. The axial proteins Hop1 and Red1 recruit the RMM complex proteins. The RMM proteins, together with the MRX, recruit and activate the Spo11 core complex that catalyses meiotic DSB formation in loops of chromatin emerging from the axis. (C) The ZMM group of proteins functions to promote meiotic crossover formation by antagonising the activity of anti-crossover factors such as the STR (Sgs1–Top3–Rmi1) complex.
Figure 2.
Figure 2.. Summary of some key meiotic recombination factors and inter-complex physical interactions in early prophase I.
Protein complexes are defined according to the convention described in the main text. Citations for the inter-complex physical interactions are; Zip3–Rad51 [6], Mer2–Mre11 [7], Red1–Zip1 [8], Red1–Zip4 [9] Mer2–Hop1 [7], Mre11–Msh5 [10], Mer3–Dmc1 [11], Mre11–Dmc1 [12].
Figure 3.
Figure 3.. Examples of key experimental protein structures of the meiotic machinery.
(A) Structures of meiotic axis proteins. Left, X-ray structure of human HORMAD1 (Hop1 in budding yeast). The N-terminal HORMA domain of HORMAD1 physically entraps the C-terminal closure motif (red) due to the movement of the safety belt (maroon) [23]. Right, the crystal structure of mouse SYCP2 N-terminus consisting of the ARM-like (ARML) and PH domains [22], C-terminal to the PH domain is a closure motif [17]. (B) CryoEM structure of the S. cerevisiae Spo11 core complex (Spo11, orange; Rec102, pale orange; Rec104, pale yellow; Ski8, grey) in complex with dsDNA (pink). The catalytic tyrosine of Spo11 (Y135) is highlighted proximal to the sugar-phosphate backbone of the dsDNA [24]. (C) cryoEM structure of human RAD51 bound to single-stranded DNA (pink) [25]. (D) Crystal structure of the human SYCP1 (Zip1 in S. cerevisiae) αN-end head-to-head assembly region [26].
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