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#ribosomes

15 public questions tagged with this topic.

Ribosome-free cytoplasmic proteins include:

Protein sorting depends on presence of N-terminal signal sequence or internal transmembrane domain. Secretory proteins like insulin, lysosomal cathepsins, plasma membrane receptors and Golgi glycosyltransferases harbor hydrophobic signals recognized by signal recognition particle leading to Sec61 engagement and translocation into ER lumen or membrane, then onward transport, removed from cytosol. Absence of signal leaves nascent chain completing synthesis on free ribosomes in cytoplasm where folding by Hsp70 and TRiC chaperonin occurs. Cytoskeletal proteins actin forty three kDa forming seven n

Ref: Blobel Nobel Lecture; signal sequence free vs membrane-bound polysomes actin spectrin cytosolic.

Which of the following proteins bind ribosomes to the rough ER?

Binding of ribosomes to rough ER ensures nascent secretory proteins directly translocate into lumen avoiding cytosolic exposure of hydrophobic stretches. This interaction requires specific receptors beyond Sec61 translocon. Ribophorin I and II are type I transmembrane glycoproteins of sixty and eighty kDa forming part of oligosaccharyltransferase complex, strongly associated with translocon. Their cytosolic domains contact sixty S subunit near polypeptide exit tunnel, increasing ribosome affinity approximately tenfold compared to naked lipid bilayer. After signal sequence inserts into Sec61 ch

Ref: Alberts Ch 12; ribophorin I/II OST subunits anchor 60S to Sec61, increase ER ribosome affinity.

During cell fractionation, a researcher identifies: Fraction X: a semi-fluid material in which numerous reactions needed

The cytoplasm is the semi-fluid matrix and principal arena of cellular reactions. Ribosomes are non-membrane-bound RNA–protein particles occurring freely in the cytoplasm, on rough ER, and within mitochondria and chloroplasts.

Ref: NCERT Class 11 Biology Chapter 8: Cell: The Unit of Life Mitochondria Plastids Ribosomes and Other Organelles