The IDENTIFICATION OF a RIBOSOMAL-BOUND Β-Glucosidase

Kihara, Hirozi K.; Hu, Ankang; Halvorson, Harlyn O.

doi:10.1073/pnas.47.4.489

Cited by 25 publications

(3 citation statements)

References 22 publications

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“…The capacity of nascent protein on ribosomes to be recognized by specific antibody has already been reported for fl-galactosidase in E. coli (Cowie et al, 1961) and for triose phosphate dehydrogenose in yeast (Warren and Goldthwait, 1962). One should mention here that a variety of enzymes, mostly in a latent form, have been found associated with ribosomal particles (Elson, 1959;Siekevitz and Palade, 1960;Cowie et al, 1961;Kihara et al, 1961;Spahr and Hollingworth, 1961;Warren and Goldthwait, 1962). It is probable that many, if not all these ribosome-bound enzymes are nascent proteins.…”

Section: Discussionmentioning

confidence: 77%

“…precipitated/mg protein mixed with antiserum, compare data in Tables 4 and 11) as purification of ribosomes progresses, speaks against a contamination as an explanation of the results obtained. In the other cases already described where specific proteins have been found in association with purified ribosomes either in bacteria or in animal and plant cells, the available evidence pointed either to nascent proteins or to intrinsic constituents of the particles (Elson, 1959;Siekevitz and Palade, 1960;Spahr and Hollingworth, 1961;Cowie et al, 1961;Kihara et al, 1961;Warren and Goldthwait, 1962). Where a control reconstruction experiment was made by mixing ribosomes lacking the protein with supernatant containing it, the results were negative (Cowie et al, 1961).…”

Section: Attachment Of Poliovirus Specific Protein To Ribosomesmentioning

confidence: 97%

See 1 more Smart Citation

Virus Specific Protein and a Ribonucleic Acid Associated with Ribosomes in Poliovirus Infected HeLa Cells

Attardi¹,

Smith²

1962

Cold Spring Harbor Symposia on Quantitative Biology

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Section: Discussionmentioning

confidence: 77%

Section: Attachment Of Poliovirus Specific Protein To Ribosomesmentioning

confidence: 97%

Virus Specific Protein and a Ribonucleic Acid Associated with Ribosomes in Poliovirus Infected HeLa Cells

Attardi¹,

Smith²

1962

Cold Spring Harbor Symposia on Quantitative Biology

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“…The cotranslational fold has been studied essentially in parallel to the description of protein synthesis by the ribosome since the middle of the last century. Early observations made it clear that some nascent chains of β-galactosidase still bound to the ribosome are enzymatically active [1]. More direct evidence that a polypeptide still attached to the ribosome, can adopt its native fold came from the use of conformational antibodies raised against β-galactosidase and tailspike protein of phage P22.…”

Section: Introductionmentioning

confidence: 99%

Comprehensive structural analysis of designed incomplete polypeptide chains of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus

2017

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The cotranslational folding is recognized as a very cooperative process that occurs after the nearly completion of the polypeptide sequence of a domain. Here we investigated the challenges faced by polypeptide segments of a non-vectorial β-barrel fold. Besides the biological interest behind the SARS coronavirus non-structural protein 1 (nsp1, 117 amino acids), this study model has two structural features that motivated its use in this work: 1-its recombinant production is dependent on the temperature, with greater solubility when expressed at low temperatures. This is an indication of the cotranslational guidance to the native protein conformation. 2-Conversely, nsp1 has a six-stranded, mixed parallel/antiparallel β-barrel with intricate long-range interactions, indicating it will need the full-length protein to fold properly. We used non-denaturing purification conditions that allowed the characterization of polypeptide chains of different lengths, mimicking the landscape of the cotranslational fold of a β-barrel, and avoiding the major technical hindrances of working with the nascent polypeptide bound to the ribosome. Our results showed partially folded states formed as soon as the amino acids of the second β-strand were present (55 amino acids). These partially folded states are different based on the length of polypeptide chain. The native α-helix (amino acids 24-37) was identified as a transient structure (~20-30% propensity). We identified the presence of regular secondary structure after the fourth native β-strand is present (89 amino acids), in parallel to the collapse to a non-native 3D structure. Interestingly the polypeptide sequences of the native strands β2, β3 and β4 have characteristics of α-helices. Our comprehensive analyses support the idea that incomplete polypeptide chains, such as the ones of nascent proteins much earlier than the end of the translation, adopt an abundance of specific transient folds, instead of disordered conformations.

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Aspects of the Biosynthesis of Enzymes

Chantrenne¹

1962

Advances in Enzymology - And Related Areas of Molecular Biology

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The IDENTIFICATION OF a RIBOSOMAL-BOUND Β-Glucosidase

Cited by 25 publications

References 22 publications

Virus Specific Protein and a Ribonucleic Acid Associated with Ribosomes in Poliovirus Infected HeLa Cells

Virus Specific Protein and a Ribonucleic Acid Associated with Ribosomes in Poliovirus Infected HeLa Cells

Comprehensive structural analysis of designed incomplete polypeptide chains of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus

Aspects of the Biosynthesis of Enzymes

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