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The murine SCP3 gene is required for synaptonemal complex assembly, chromosome synapsis, and male fertility.
A null mutation in the SCP3 gene was generated, and it was noted that homozygous mutant males were sterile due to massive apoptotic cell death during meiotic prophase, and a residual chromatin organization remained in the mutant meiotic cells. Expand
A nuclear cap-binding complex binds Balbiani ring pre-mRNA cotranscriptionally and accompanies the ribonucleoprotein particle during nuclear export
It is demonstrated that CBP20 binds to the nascent pre-mRNA shortly after transcription initiation, stays in the RNP particles after splicing has been completed, and remains attached to the 5' domain during translocation of the R NP through the nuclear pore complex (NPC). Expand
Localization of the N-terminus of SCP1 to the central element of the synaptonemal complex and evidence for direct interactions between the N-termini of SCP1 molecules organized head-to-head.
It is suggested that a transversal filament consists of one or more pairs of SCP1 dimers, each pair being organized in a head-to-head arrangement with the C-termini anchored in the lateral elements and the two N- termini being joined in the central element. Expand
The Synaptonemal Complex Protein SCP3 Can Form Multistranded, Cross-striated Fibers In Vivo
It is proposed that SCP3 fibers constitute the core of the lateral elements of the synaptonemal complex and function as a molecular framework to which other proteins attach, regulating DNA binding to the chromatid axis, sister Chromatid cohesion, synapsis, and recombination. Expand
Translocation of a specific premessenger ribonucleoprotein particle through the nuclear pore studied with electron microscope tomography
A specific premessenger ribonucleoprotein (RNP) particle in the salivary glands of the dipteran Chironomus tentans was studied with electron microscope tomography during translocation from the cellExpand
A Pre-mRNA-Binding Protein Accompanies the RNA from the Gene through the Nuclear Pores and into Polysomes
It is demonstrated that hrp36 is added to BR RNA concomitant with transcription, remains in nucleoplasmic BR particles, and is translocated through the nuclear pore still associated with BR RNA. Expand
Actin Bound to the Heterogeneous Nuclear Ribonucleoprotein Hrp36 Is Associated with Balbiani Ring mRNA from the Gene to Polysomes
It is demonstrated by cross linking that nuclear as well as cytoplasmic actin are bound to hrp36 in vivo, and it is concluded that actin is likely to be bound to the BR transcript via hrp 36 during the transfer of the mRNA from the gene all the way into polysomes. Expand
An actin–ribonucleoprotein interaction is involved in transcription by RNA polymerase II
The results indicate that an actin-based mechanism is implicated in the transcription of most if not all RNA polymerase II genes and suggest that anActin–hrp65-2 interaction is required to maintain the normal transcriptional activity of the cell. Expand
The central region of the synaptonemal complex revealed in three dimensions.
The synaptonemal complex plays a key role in pairing of homologous chromosomes during meiosis. Its gross structure was already known by conventional electron microscopy, but only recently has it beenExpand
Simulation of transmission electron microscope images of biological specimens
The simulator has been designed to provide a platform for development of new instrumentation and image processing procedures in single particle electron microscopy, two‐dimensional crystallography and electron tomography with well documented protocols and an open source code into which new improvements and extensions are easily incorporated. Expand