The N-terminal amino acid sequence of the small subunit of ribulose-1,5-diphosphate carboxylase fromNicotiana tabacum

Gibbons, Gregory C.; Strøbæk, Steffen; Haslett, Barry G.; Boulter, D.

doi:10.1007/bf02326947

Cited by 17 publications

(6 citation statements)

References 10 publications

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“…MethGln-Val-Trp-Pro-pro-(Tyr( Asn Lys-Lys-Lys-Tyr-RIle )~Glyj R. rubrum carboxylase Met-Asp-Gln-Ser-Ser-Arg-Tyr-Val-Asn-Leu-Ala-Leu-Lys-Glu-Glu-Asp-Leu-Ile-Ala-Gly-Gly-Glx-His-Val-L';u-' Data of Gibbons et al (15), Str0baek et al (61), and Iwai et al (20).…”

Section: Spinach Large Subunitunclassified

Isolation, characterization, and crystallization of ribulosebisphosphate carboxylase from autotrophically grown Rhodospirillum rubrum

Schloss¹,

Phares²,

Long³

et al. 1979

J Bacteriol

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Serial culture of Rhodospirillum rubrum with 2% CO2 in H2 as the exclusive carbon source resulted in a rather large fraction of the soluble protein (>40%) being comprised of ribulosebisphosphate carboxylase (about sixfold higher than the highest value previously reported). Isolation of the enzyme from these cells revealed that it has physical and kinetic properties similar to those previously described for the enzyme derived from cells grown on butyrate. Notably, the small subunit (which is a constituent of the carboxylase from eucaryotes and most procaryotes) was absent in the enzyme from autotrophically grown R. rubrum. Edman degradation of the purified enzyme revealed that the NH2 terminus is free (in contrast to the catalytic subunit of the carboxylase from eucaryotes) and that the NH2-terminal sequence is Met-

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Section: Spinach Large Subunitunclassified

Isolation, characterization, and crystallization of ribulosebisphosphate carboxylase from autotrophically grown Rhodospirillum rubrum

Schloss¹,

Phares²,

Long³

et al. 1979

J Bacteriol

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“…This difference is unlikely to be the result of partial proteolytic cleavage during extraction and purification, since this might be expected to produce a "ragged" N-terminus and overlapping sequences, as has been observed in several higher plant species. For example, Nicotiana tabacum partially loses the N-terminal methionine residue (Gibbons et al 1975), leading to two sequences displaced by one residue. In the present investigation there was no "ragged end" to the molecule, and only one amino acid was observed in each position.…”

Section: Discuss I 0 Nmentioning

confidence: 99%

AMINO ACID SEQUENCE ANALYSIS OF THE SMALL SUBUNIT OF RIBULOSE BISPHOSPHATE CARBOXYLASE FROM FUCUS (PHAEOPHYCEAE)¹

Keen

Pappin

Evans

1988

Journal of Phycology

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This paper reports for the first time amino acid sequence information for the small subunit of ribulose‐1,5‐bisphosphate carboxylase / oxygenase (Rubisco) from a non‐green alga. N‐terminal sequences are presented for the polypeptide from three species of the genus Fucus (Phaeophyceae). Although homologous to small subunit polypeptides from other organisms, the Fucus sequences exhibit a unique N‐terminal section resembling neither cyanobacterial nor chlorophytic sequences. This difference may be a consequence of the plastid DNA coding arrangement for the small subunit in chromophytes, a situation reported for the related organism Olisthodiscus but not previously investigated at the amino acid sequence level.

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“…Previous comparisons have shown that the amino acid composition of the small subunit exhibits considerable inter-specific variation. Automatic determination of the N-terminal sequence of the small subunits from barley, pea, bean, and tobacco (10,13,31) have shown that the small subunits are homologous polypeptides but with a substantial number of amino acid substitutions between them. As shown in Table II the amino acid compositions of the large subunits are very similar between the species confirming that these are also homologous polypeptides but which are too large for small differences between them to be resolved by amino acid analysis.…”

Section: Studies On the Subunits Of Rudp Carboxylasementioning

confidence: 99%

Ribulose 1,5-diphosphate carboxylase from Oenothera. Purification and a peptide mapping procedure for the subunits

Holder

1976

Carlsberg Res. Commun.

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Ribulose 1,5-diphosphate carboxylase has been purified from fully expanded leaves of Oenothera. The isolation procedure overcame the problems which resulted from a high content of mucilage and phenolic compounds in the leaves. Protein extraction into dilute buffer containing a phenol adsorbant and reducing agents followed by a combination of gel filtration and ion exchange chromatography allowed the enzyme to be essentially purified to homogeneity. The purified RuDP carboxylase had a specific activity of 1.5 i.tmoles CO2 fixed, min -~. mg -~ at pH 7.8 and 25 ~ The two subunits could be dissociated in detergent solutions and were found to have molecular weights and amino acid compositions similar to the respective subunits from other sources. A two-dimensional mapping procedure employing ion exchange and paper chromatography was used to partially characterize the tryptic peptides of the RuDP carboxylase subunits; this technique may be useful in interspecific comparisons of the primary structure of the two subunits from Oenothera species.

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The N-terminal amino acid sequence of the small subunit of ribulose-1,5-diphosphate carboxylase fromNicotiana tabacum

Cited by 17 publications

References 10 publications

Isolation, characterization, and crystallization of ribulosebisphosphate carboxylase from autotrophically grown Rhodospirillum rubrum

Isolation, characterization, and crystallization of ribulosebisphosphate carboxylase from autotrophically grown Rhodospirillum rubrum

AMINO ACID SEQUENCE ANALYSIS OF THE SMALL SUBUNIT OF RIBULOSE BISPHOSPHATE CARBOXYLASE FROM FUCUS (PHAEOPHYCEAE)¹

Ribulose 1,5-diphosphate carboxylase from Oenothera. Purification and a peptide mapping procedure for the subunits

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The N-terminal amino acid sequence of the small subunit of ribulose-1,5-diphosphate carboxylase fromNicotiana tabacum

Cited by 17 publications

References 10 publications

Isolation, characterization, and crystallization of ribulosebisphosphate carboxylase from autotrophically grown Rhodospirillum rubrum

Isolation, characterization, and crystallization of ribulosebisphosphate carboxylase from autotrophically grown Rhodospirillum rubrum

AMINO ACID SEQUENCE ANALYSIS OF THE SMALL SUBUNIT OF RIBULOSE BISPHOSPHATE CARBOXYLASE FROM FUCUS (PHAEOPHYCEAE)1

Ribulose 1,5-diphosphate carboxylase from Oenothera. Purification and a peptide mapping procedure for the subunits

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AMINO ACID SEQUENCE ANALYSIS OF THE SMALL SUBUNIT OF RIBULOSE BISPHOSPHATE CARBOXYLASE FROM FUCUS (PHAEOPHYCEAE)¹