Sequence of the human 40-kDa keratin reveals an unusual structure with very high sequence identity to the corresponding bovine keratin

Journal Article · Mon Feb 01 00:00:00 EST 1988 · Proc. Natl. Acad. Sci. U.S.A.; (United States)

DOI:https://doi.org/10.1073/pnas.85.4.1114· OSTI ID:6879605

Eckert, R L

The complete amino acid and DNA sequences of the human 40-kDa keratin are reported. The DNA sequence encodes a protein of 44,098 Da, which is unique in that it lacks the terminal non-..cap alpha..-helical tail segment found in all other keratins. When the human 40-kDa keratin amino acid sequence is compared to the corresponding bovine keratin, the overall identity is 89%. The coil-forming regions are 89% identical and the head regions are 88% identical. This similarity is also evident in the DNA sequence of the coding region, the 5' upstream sequences, and the 3' noncoding sequences. The high degree of cross-species identity between bovine and human 40-kDa keratins suggests that there is strong evolutionary pressure to conserve the structure of this keratin. This in turn suggests an important and universal role for this intermediate filament subunit in all species.

• Research Organization: Case Western Reserve Univ. School of Medicine, Cleveland, OH (USA)
• OSTI ID: 6879605
• Journal Information: Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 85:4
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
KERATIN
AMINO ACID SEQUENCE
BIOLOGICAL EVOLUTION
CATTLE
DNA SEQUENCING
MAN
PHOSPHORUS 32
RECOMBINANT DNA
ANIMALS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
DAYS LIVING RADIOISOTOPES
DNA
DOMESTIC ANIMALS
ISOTOPES
LIGHT NUCLEI
MAMMALS
MOLECULAR STRUCTURE
NUCLEI
NUCLEIC ACIDS
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
PHOSPHORUS ISOTOPES
PRIMATES
PROTEINS
RADIOISOTOPES
RUMINANTS
SCLEROPROTEINS
STRUCTURAL CHEMICAL ANALYSIS
VERTEBRATES
550201* - Biochemistry- Tracer Techniques