Hh. Offenberg et al., SCP2 - A MAJOR PROTEIN-COMPONENT OF THE AXIAL ELEMENTS OF SYNAPTONEMAL COMPLEXES OF THE RAT, Nucleic acids research, 26(11), 1998, pp. 2572-2579
In the axial elements of synaptonemal complexes (SCs) of the rat, majo
r protein components have been identified, with relative electrophoret
ic mobilities (M(r)s) of 30 000-33 000 and 190 000. Using monoclonal a
nti-SC antibodies, we isolated cDNA fragments which encode the 190 000
M-r component of rat SCs, The translation product predicted from the
nucleotide sequence of the cDNA, called SCP2 (for synaptonemal complex
protein 2), is a basic protein (pl = 8.0) with a molecular mass of 17
3 kDa, At the C-terminus, a stretch of similar to 50 amino acid residu
es is predicted to be capable of forming coiled-coil structures. SCP2
contains two clusters of S/T-P motifs, which are common in DNA-binding
proteins. These clusters flank the central, most basic part of the pr
otein (pl = 9.5). Three of the Sla-P motifs are potential target sites
for p34(cdc2) protein kinase, In addition, SCP2 has eight potential c
AMP/cGMP-dependent protein kinase target sites. The gene encoding SCP2
is transcribed specifically in the testis, In meiotic prophase cells.
At the amino acid sequence and secondary structural level, SCP2 shows
some similarity to the Red1 protein, which is involved in meiotic rec
ombination and the assembly of axial elements of SCs in yeast. We spec
ulate that SCP2 is a DNA-binding protein involved in the structural or
ganization of meiotic prophase chromosomes.