plastid PEP RNA polymerase core enzyme binding

Binding to a bacterial-type plastid PEP RNA polymerase core enzyme, typically consisting of two alpha, one beta, one beta prime, and one double prime subunit.

cytoplasmic exosome (RNase complex)

A ribonuclease complex that has 3-prime to 5-prime processive hydrolytic exoribonuclease activity producing 5-prime-phosphomonoesters. Participates in a multitude of cellular RNA processing and degradation events preventing nuclear export and/or translation of aberrant RNAs. Restricted to processing linear and circular single-stranded RNAs (ssRNA) only. RNAs with complex secondary structures may have to be unwound or pre-processed by co-factors prior to entering the complex, esp if the 3-prime end is structured.

exosome (RNase complex)

A ribonuclease complex that has 3-prime to 5-prime exoribonuclease activity and possibly endoribonuclease activity, producing 5-prime-phosphomonoesters. Participates in a multitude of cellular RNA processing and degradation events preventing nuclear export and/or translation of aberrant RNAs. Restricted to processing linear and circular single-stranded RNAs (ssRNA) only. RNAs with complex secondary structures may have to be unwound or pre-processed by co-factors prior to entering the complex, esp if the 3-prime end is structured.

nuclear exosome (RNase complex)

A ribonuclease complex that has 3-prime to 5-prime processive and distributive hydrolytic exoribonuclease activity and endoribonuclease activity, producing 5-prime-phosphomonoesters. Participates in a multitude of cellular RNA processing and degradation events preventing nuclear export and/or translation of aberrant RNAs. Restricted to processing linear and circular single-stranded RNAs (ssRNA) only. RNAs with complex secondary structures may have to be unwound or pre-processed by co-factors prior to entering the complex, esp if the 3-prime end is structured.

nucleolar exosome (RNase complex)

A ribonuclease complex that has 3-prime to 5-prime distributive hydrolytic exoribonuclease activity and in some taxa (e.g. yeast) endoribonuclease activity, producing 5-prime-phosphomonoesters. Participates in a multitude of cellular RNA processing and degradation events preventing nuclear export and/or translation of aberrant RNAs. Restricted to processing linear and circular single-stranded RNAs (ssRNA) only. RNAs with complex secondary structures may have to be unwound or pre-processed by co-factors prior to entering the complex, esp if the 3-prime end is structured.

bacterial-type RNA polymerase core enzyme binding

Binding to a bacterial-type RNA polymerase core enzyme, typically consisting of two alpha, one beta, one beta prime, and one omega subunit.

lipopolysaccharide immune receptor activity

Combining with a lipopolysaccharide and transmitting the signal across the cell membrane to initiate an innate immune response. Lipopolysaccharides (LPS) are major components of the outer membrane of Gram-negative bacteria, making them prime targets for recognition by the immune system.

suture of dorsal opening

Closure of the dorsal hole. Filopodia extending from each leading edge interdigitate at the dorsal midline and appear to prime the formation of adherens junctions between the two rows of leading edge cells. Newly formed septate junctions are also used to seal the dorsal hole.

cytosolic DNA-directed RNA polymerase complex

The eubacterial DNA-directed RNA polymerase is a multisubunit complex with a core composed of the essential subunits beta-prime, beta, and two copies of alpha and a fifth nonessential subunit called omega. An additional subunit, a sigma factor, is required for promoter recognition and specificity.

plastid-encoded plastid RNA polymerase complex

An RNA polymerase complex containing polypeptides encoded by the plastid genome. Plastid-encoded DNA-directed RNA polymerases resemble eubacterial multisubunit RNA polymerases, with a core composed of alpha, beta, and beta-prime subunits. Some forms contain multiple additional subunits. An additional sigma factor subunit is required for promoter recognition.