Amino-terminal sequences of the L,M, and H subunits of reaction centers from the photosynthetic bacterium Rhodopseudomonas sphaeroides R-26

Journal Article · Fri Jan 01 04:00:00 EST 1982 · Biochemistry; (United States)

DOI:https://doi.org/10.1021/bi00259a019· OSTI ID:6123793

Sutton, M R ^[1]; Rosen, D; Feher, G; Steiner, L A

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1. Massachusetts Inst. of Tech., Cambridge

We have determined the sequence of the 25-28 amino-terminal residues of the three subunits, L,M, and H, of the membrane-bound reaction center protein of the photosynthetic bacterium Rhodopseudomonas sphaeroides R-26. The sequences are as follows: L, H/sub 2/N-Ala-Leu-Leu-Ser-Phe-Glu-Arg-Lys-Tyr-Arg-Val-Pro-Gly-Gly-Thr-Leu-Val-Gly-Gly-Asn-Leu-Phe-Asp-Phe-(His)-Val-; M, H/sub 2/N-Ala-Glu-Tyr-Gln-Asn-Ile-Phe-Ser-Gln-Val-Gln-Val-Arg-Gly-Pro-Ala-Asp-Leu-Gly-Met-Thr-Glu-Asp-Val-Asn-Leu-Ala-Asn-; H, H/sub 2/N-Met-Val-Gly-Val-Thr-Ala-Phe-Gly-Asn-Phe-Asp-Leu-Ala-Ser-Leu-Ala-Ile-Tyr-Ser-Phe-Trp-Ile-Phe-Leu-Ala-X-Leu-Ile-. The H sequence, especially after the aspartyl residue at position 11, is rich in hydrophobic residues, consistent with the possibility that this section of the polypeptide chain is located within the membrane. The L sequence is hydrophilic near the amino terminus and then becomes moderately hydrophobic. The M sequence is of average polarity.

• OSTI ID: 6123793
• Journal Information: Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 21; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
550700 -- Microbiology
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
BACTERIA
CARBOXYLIC ACIDS
CELL CONSTITUENTS
CELL MEMBRANES
MEMBRANES
MICROORGANISMS
ORGANIC ACIDS
ORGANIC COMPOUNDS
PHOTOSYNTHETIC BACTERIA
PROTEINS
RHODOPSEUDOMONAS
STRUCTURAL CHEMICAL ANALYSIS