Honorifics and politeness in Korean

국문 초록 (Abstract)

언어에서 존대법과 공손법을 나타내 주는 방법은 실로 다양하다. 한국어는 존대-공손법을 언어체계내에서 발 표현해 주는 언어 중 하나이다. 본 논문은 한국어에 나타나고 있는 존대-공손법과 관련된 이론과 요인을 사회언어학적 관점에서 고찰해 보고자 한다. 본 논문의 구성은 다음과 같다.
제1장. 서론
제2장. 존대법
제3장. 공손법
제4장. 한국어의 친족어

제2장에서는 한국어의 존대법을 청자와 관련하여 다음과 같이 크게 세 부류로 나눈다: 청자 존대, 주체존대 그리고 객체 존대. 이장에서는 담화의 주요 참여자인 화자-주체-객체-청자 둘간의 상호 관계가 적절한 존대법 설정의 근거가 됨을 다양한 예를 통하여 밝히고 한국어의 존대체계를 확립한다.

3장에서는 존대법의 사용과 관련하여 공손법의 역할을 고찰한다. "공손"에 대한 기존 연구의 문제점을 기술하고 Gricean Maxims로 비롯된 대화함축(conversational implicature)의 관점에서 공손법에 대한 새로운 정의를 시도한다. 특히 3장의 마지막 절에서는 사회-문화적인 관점에서 한국어의 공손법을 재조명해 본다.

마지막 4장은 한국어 친족어와 관련된 존대-공손법을 고찰한다. 한국의 친족관계와 관련된 언어적 특질을 기술하고 특히, 친족관계에 있어서 호칭표현과 지칭표현이 어떻게 공손법과 긴밀히 연관되는지를 면밀히 분석할 것이다.

다국어 초록 (Multilingual Abstract)

The bacteriophage λO protein localizes the initiation of replication to a unique sequence, ori λ through specific protein-DNA and protein-protein interactions.
Conformational changes at ori λ introduced by O protein binding have been reported and their roles have been implicated in the initiation of λ DNA replication. In our studies, we focused on detailed structural basis of the formation of the O protein-ori λ complex(O-some). This work was divided into five Chapters including a general introduction given in Chapter 1, a brief review of genetic, biochemical, and structural data for understanding the mechanism of the initiation of λ DNA replication. As shown in Chapter 2, we found that the O protein exists as a dimer and demonstrated that the active DNA binding species is also a dimer. Dimerization and sequence-specific DNA recognition are specifically mediated through the amino-terminal half of O(O1-162(아래첨자 1-162입력불가)). The binding affinity of O for a single copy of its 19 bp recognition sequence was 2-3 nM.
We also found that the O-some is composed of 4 dimers of O and ori λ DNA, which contains four 19 bp direct repeat recognition sites, i, e., a dimer of O is bound to each repeat(iteron). Moreover, we found that only the amino-terminal DNA binding domain is required for formation of the O-some.
To investigate the structural basis for the unique properties of O protein, we generated a number of carboxy-terminal and internal and internal deletion mutants of O. Experiments with purified mutant proteins, as shown in Chapter 3, indicated that (ⅰ) the deletion mutant retaining amino acid residues 19-110 is the smallest O protein species that can both bind to DNA and form a dimer, (ⅱ) the affinities of all mutant proteins for a single iteron are almost the same, ranging from 2 to 4 nM; (ⅲ) the portion of O that is responsible for dimerization is located between amino acid residues 19 and 85; (ⅳ) the carboxy-terminal domain (O 156-299(아래첨자 156-299입력불가)) is a monomeric species that does not recognize specific DNA sequences but instead, bind non-specifically to duplex DNA; (ⅴ) the linker joining the two structural domains is not required for O function, but its coding sequence of DNA contains several recognition sites for O protein (ori λ); and (ⅵ) a deletion!
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utant missing the amino-terminal portion of the carboxyl-terminal domain is still comparably active in the in vitro λdv replication assay.
In Chapter 4, the structural basis of the O protein-DNA complex was studied in detail. Hydroxy radical footprinting was employed to obtain the high resolution structural information about the contacts between the protein and the sugar-phosphate backbone of DNA. The missing nucleoside experiment allowed us to identify energetically important base moieties that may be in contact with bound O protein.
Quantitation of the extent of O-mediated DNA bending indicated that O induces a relatively sharp bend in an individual recognition sequence of 85。 ±5。 . Measurement of the O-induced topological change indicated that a region of DNA or specifically ori λis wrapped around the O protein core in a left-handed fashion with a linking number change of 0.7±0.1 turn.
In Chapter 5, we present direct evidence that the O protein also has the capacity to interact with single-stranded DNA, the first such interaction discovered among prokaryotic origin-binding proteins. The implication of this dual DNA binding specificity of O for the formation of the unwound structure at the A/T-rich region of ori λ is dis cussed. The addition of the λP-DnaB comple x to the O-some produces a new nucleoprotein species with a super-shift in migration. The presence of P and DnaB reduces significantly the amount of O required for binding to single-stranded DNA.
Based on these results, we propose a detailed model for sequential structural changes in ori λ as a consequence of O binding to the origin of λreplication.